SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing BWI76_RS00670 FitnessBrowser__Koxy:BWI76_RS00670 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 4 hits to proteins with known functional sites (download)

1gt7A L-rhamnulose-1-phosphate aldolase from escherichia coli (see paper)
88% identity, 99% coverage: 1:274/276 of query aligns to 1:274/274 of 1gt7A

query
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1gt7A

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active site: E117 (= E117), H141 (= H141), H143 (= H143), E171 (= E171), H212 (= H212)
binding phosphoglycolohydroxamic acid: N29 (= N29), G30 (= G30), G31 (= G31), N32 (= N32), S75 (= S75), G76 (= G76), T115 (= T115), S116 (= S116), E117 (= E117), H141 (= H141), H143 (= H143), H212 (= H212)
binding zinc ion: H141 (= H141), H143 (= H143), H212 (= H212)

P32169 Rhamnulose-1-phosphate aldolase; EC 4.1.2.19 from Escherichia coli (strain K12) (see 2 papers)
88% identity, 99% coverage: 1:274/276 of query aligns to 1:274/274 of P32169

query
sites
P32169

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R28 (= R28) mutation R->A,S: Severe loss of enzymatic activity.
N29 (= N29) mutation to A: Severe loss of enzymatic activity.
E117 (= E117) active site; mutation to Q: Loss of enzymatic activity.
H141 (= H141) binding
H143 (= H143) binding
E171 (= E171) mutation E->S,A,Q: Loss of enzymatic activity.
E192 (= E192) mutation to A: No effect on enzymatic activity.
H212 (= H212) binding

1ojrA L-rhamnulose-1-phosphate aldolase from escherichia coli (mutant e192a) (see paper)
88% identity, 99% coverage: 1:274/276 of query aligns to 1:274/274 of 1ojrA

query
sites
1ojrA

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active site: E117 (= E117), H141 (= H141), H143 (= H143), E171 (= E171), H212 (= H212)
binding Dihydroxyacetone: N29 (= N29), G30 (= G30), G31 (= G31), N32 (= N32), E117 (= E117), H141 (= H141), H143 (= H143), H212 (= H212)
binding phosphate ion: N29 (= N29), N32 (= N32), N32 (= N32), S75 (= S75), G76 (= G76), T115 (= T115), S116 (= S116), E117 (= E117), H141 (= H141), H212 (= H212)
binding zinc ion: H141 (= H141), H143 (= H143), H212 (= H212)

2v9mA L-rhamnulose-1-phosphate aldolase from escherichia coli (mutant a87m- t109f-e192a) (see paper)
87% identity, 99% coverage: 1:274/276 of query aligns to 1:274/274 of 2v9mA

query
sites
2v9mA

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active site: E117 (= E117), H141 (= H141), H143 (= H143), E171 (= E171), H212 (= H212)
binding calcium ion: E200 (≠ A200), H204 (= H204)
binding zinc ion: H141 (= H141), H143 (= H143), H212 (= H212)

Query Sequence

>BWI76_RS00670 FitnessBrowser__Koxy:BWI76_RS00670
MQTIIDAWFVQGMIKATSDAWLKGWDERNGGNLTLRLDEADIEPYAADFHAKPRYIALSQ
PMPTLANQPFIVTGSGKFFRNVQLDPAANLGVVKVDSDGAGYHILWGLTNDAVPTSELPA
HFLSHSERIKLTNGKDRVIMHCHATNLIALTYVLENSSDLFTRKLWEGSTECLVVFPDGV
GILPWMVPGTDEIGQATAEAMQKHSLVLWPFHGVFGSGPNLDETFGLIDTAEKSAEVLVK
VYSMGGMKQTITREELIALGKRFNVHPLQSALDLYQ

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