SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing Echvi_3158 FitnessBrowser__Cola:Echvi_3158 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 6 hits to proteins with known functional sites (download)

P0A991 Fructose-bisphosphate aldolase class 1; Fructose-bisphosphate aldolase class I; FBP aldolase; EC 4.1.2.13 from Escherichia coli (strain K12) (see 2 papers)
61% identity, 99% coverage: 6:353/353 of query aligns to 3:350/350 of P0A991

query
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P0A991

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K208 (= K211) modified: N6-acetyllysine
K237 (= K240) active site, Schiff-base intermediate with dihydroxyacetone-P; mutation to A: Loss of activity.
K239 (= K242) mutation to A: No change in activity.
K262 (≠ T265) modified: N6-acetyllysine

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

P58315 Fructose-bisphosphate aldolase class 1; Fructose-bisphosphate aldolase class I; FBP aldolase; FBPA; EC 4.1.2.13 from Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1) (see paper)
28% identity, 73% coverage: 73:329/353 of query aligns to 20:237/263 of P58315

query
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P58315

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W144 (= W202) mutation to E: Loss of FBP aldolase activity; when associated with F-146.
Y146 (= Y204) mutation to F: The catalytic activity is at least 3-fold lower than for the wild-type. Loss of FBP aldolase activity; when associated with E-144.

2yceE Structure of an archaeal fructose-1,6-bisphosphate aldolase with the catalytic lys covalently bound to the carbinolamine intermediate of the substrate. (see paper)
28% identity, 73% coverage: 73:329/353 of query aligns to 18:235/255 of 2yceE

query
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binding d-mannitol-1,6-diphosphate: D22 (= D77), H23 (≠ Q78), H27 (= H82), W142 (= W202), R146 (= R206), K175 (= K240), K177 (= K242), G201 (= G293), G202 (= G294), V228 (≠ M322), G229 (= G323), R230 (= R324)

1w8sA The mechanism of the schiff base forming fructose-1,6-bisphosphate aldolase: structural analysis of reaction intermediates (see paper)
28% identity, 73% coverage: 73:329/353 of query aligns to 18:235/250 of 1w8sA

query
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1w8sA

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binding 1,6-di-O-phosphono-beta-D-fructofuranose: A20 (≠ P75), D22 (= D77), H23 (≠ Q78), H27 (= H82), R146 (= R206), K175 (= K240), K177 (= K242), S200 (= S292), G201 (= G293), G202 (= G294), V228 (≠ M322), G229 (= G323), R230 (= R324)

P58314 Fructose-bisphosphate aldolase class 1; Fructose-bisphosphate aldolase class I; FBP aldolase; EC 4.1.2.13 from Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) (see paper)
25% identity, 74% coverage: 69:329/353 of query aligns to 21:251/281 of P58314

query
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P58314

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K191 (= K240) mutation to A: Loss of activity.

2qjgA M. Jannaschii adh synthase complexed with f1,6p (see paper)
21% identity, 75% coverage: 73:335/353 of query aligns to 29:249/272 of 2qjgA

query
sites
2qjgA

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binding 1,6-di-o-phosphono-d-allitol: H34 (≠ Q78), S37 (≠ E81), Y153 (= Y204), R155 (= R206), K184 (= K240), G209 (≠ S292), G210 (= G293), V236 (≠ M322), G237 (= G323), R238 (= R324)

Query Sequence

>Echvi_3158 FitnessBrowser__Cola:Echvi_3158
MKTDKNIVELLGEKASFYLEHICEKITKDELQTPSKNSIDKVFGNSNRNPQVLRSLSQLY
NHGNLAGTGYLSILPVDQGIEHSAAYSFYKNPDYFDPENIIKLALEAGCNGVASTFGVLG
LNARKYAHKIPFIVKINHNELLTYPNKYDQTLFGKVKTAWDMGAIAVGATIYFGSAESNR
QLKEIAEAFEEAHNLGMATILWCYTRNEAFKTEKEDYHAAADVTGQANHLGVTIQADIIK
QKLPTNNFGFKEIGFGKYDDEMYKTLTTDHPIDLCRLQVANCYMGKIGLINSGGGSKGES
DLVEAITTAVINKRAGGSGLIMGRKAFQKPFTEGIELLRFVQDVYLDQKISIA

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