SitesBLAST
Comparing WP_011951434.1 NCBI__GCF_000016765.1:WP_011951434.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 3 hits to proteins with known functional sites (download)
Q72X44 Homoserine O-acetyltransferase; HAT; Homoserine transacetylase; HTA; EC 2.3.1.31 from Bacillus cereus (strain ATCC 10987 / NRS 248) (see paper)
43% identity, 93% coverage: 1:294/317 of query aligns to 1:299/301 of Q72X44
- K47 (= K47) mutation to M: 17-fold increase in Km for acetyl-CoA and 14-fold decrease in catalytic activity.; mutation to R: 7-fold increase in Km for acetyl-CoA.
- E111 (= E111) mutation to G: No activity with acetyl-CoA but catalyzes an acyltransferase reaction using succinyl-CoA and homoserine.
- C142 (= C142) mutation C->A,S: Lack of activity.
- K163 (= K163) binding substrate; mutation to M: 13-fold increase in Km for homoserine.
- S192 (= S192) binding substrate; mutation to A: 5-fold increase in Km for homoserine.
- H235 (= H235) mutation H->A,N,Q: Lack of activity.
- E237 (= E237) mutation to A: 65-fold decrease in catalytic activity.; mutation to D: 6-fold decrease in catalytic activity.; mutation to Q: 19-fold decrease in catalytic activity.
- R249 (= R249) binding substrate; mutation to M: 64-fold increase in Km for homoserine and 10-fold decrease in catalytic activity.
P07623 Homoserine O-succinyltransferase; HST; Homoserine transsuccinylase; HTS; EC 2.3.1.46 from Escherichia coli (strain K12) (see 4 papers)
42% identity, 93% coverage: 1:296/317 of query aligns to 1:301/309 of P07623
- M1 (= M1) modified: Initiator methionine, Removed
- K46 (≠ N46) mutation to A: 16-fold decrease in Km for L-homoserine. 32-fold decrease in catalytic activity.; mutation to L: 6-fold increase in Km for L-homoserine and in Km for succinyl-CoA. Slight increase in catalytic activity.; mutation to R: Slight decrease in catalytic activity.
- KK 46:47 (≠ NK 46:47) mutation to AA: Lack of activity.
- K47 (= K47) mutation to A: 22-fold decrease in Km for L-homoserine. Almost loss of catalytic activity.; mutation to L: 8-fold decrease in Km for L-homoserine and 10-fold increase in Km for succinyl-CoA. 20-fold decrease in catalytic activity.; mutation to R: 14-fold decrease in Km for L-homoserine. 72-fold decrease in catalytic activity.
- C90 (≠ R90) mutation C->A,S: No change in activity.
- C142 (= C142) mutation C->A,S: Lack of activity.
- K157 (= K157) mutation to L: Lack of activity.
- R193 (= R193) mutation to A: 3-fold increase in Km for L-homoserine. 8-fold decrease in catalytic activity.; mutation to K: 8-fold decrease in catalytic activity.
- H235 (= H235) mutation H->A,N: Lack of activity.
- E237 (= E237) mutation to A: 32-fold decrease in catalytic activity.; mutation to D: 3-fold decrease in catalytic activity.
- Y238 (= Y238) mutation to F: 5-fold increase in Km for L-homoserine.
- E246 (= E246) mutation to A: 150-fold increase in Km for L-homoserine.; mutation to D: 24-fold increase in Km for L-homoserine.
- R249 (= R249) mutation to K: 4-fold increase in Km for L-homoserine.
2vdjA Crystal structure of homoserine o-acetyltransferase (meta) from bacillus cereus with homoserine (see paper)
41% identity, 85% coverage: 17:286/317 of query aligns to 1:262/268 of 2vdjA
Query Sequence
>WP_011951434.1 NCBI__GCF_000016765.1:WP_011951434.1
MPIKIPDDLPARPILEQEGVVVMRRTDAVRQDIRPLRIGLLNLMPNKISTETQLARLLGA
TPLQVELTLVRMTDHVARHTPADHMAAFYRPWAEVRDERFDGFVITGAPVEHLPFEEVGY
WPELCRVLDWTQTHVHSSFTICWAAQAALHHFHGVPKHLLPAKAFGLFRHRNLAPASPYL
RGFSDDPHIPVSRWAEIRQADIPAGSGLETLLDSAETGPCLLDDPAHRSLHMFNHVEYDT
RSLADEYFRDGQGPLPAGYFPGDDPARPPENRWRGHAHLLFGNWINEIYRTTPFDIAAIG
GGRPPANDAGPIEAAAG
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