SitesBLAST
Comparing RR42_RS10970 FitnessBrowser__Cup4G11:RR42_RS10970 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 12 hits to proteins with known functional sites (download)
6voqA Crystal structure of ygbl, a putative aldolase/epimerase/decarboxylase from klebsiella pneumoniae
49% identity, 90% coverage: 3:192/212 of query aligns to 3:193/207 of 6voqA
Q58813 L-fuculose phosphate aldolase; L-fuculose-1-phosphate aldolase; EC 4.1.2.17 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
30% identity, 85% coverage: 8:188/212 of query aligns to 3:175/181 of Q58813
- N25 (= N30) mutation to L: It shows a 3-fold increase of the affinty for dihydroxyacetone phosphate (DHAP) and a 3-fold decrease of the affinity for DL-glyceraldehyde compared to the wild-type.; mutation to T: It shows a 5-fold decrease of the affinty for dihydroxyacetone phosphate (DHAP), but has the same affinity for DL-glyceraldehyde compared to the wild-type.
P0AB87 L-fuculose phosphate aldolase; D-ribulose-phosphate aldolase; L-fuculose-1-phosphate aldolase; EC 4.1.2.17 from Escherichia coli (strain K12) (see 4 papers)
30% identity, 96% coverage: 7:209/212 of query aligns to 6:207/215 of P0AB87
- T26 (≠ S27) mutation to A: Decrease of the aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).
- A27 (= A28) mutation Missing: Strong decrease of the aldolase activity.
- GN 28:29 (= GN 29:30) binding
- N29 (= N30) mutation to L: Loss of aldolase activity; when associated with A-71.; mutation to Q: Strong decrease of the aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).
- TG 43:44 (≠ TD 44:45) binding
- S71 (= S72) mutation to A: Loss of aldolase activity; when associated with L-29.; mutation to Q: Loss of aldolase activity.
- SS 71:72 (≠ SK 72:73) binding
- E73 (≠ T74) active site, Proton donor/acceptor; binding ; mutation to Q: Loss of aldolase activity; when associated with F-113 and F-209.; mutation to S: Loss of aldolase activity.
- H92 (= H93) binding
- H94 (= H95) binding
- Y113 (= Y120) Plays a key role in the stabilization of the transition state and positioning the aldehyde component; mutation to F: Slowly inactivated. Has a preference for the D-aldehyde and shows an inversion of the diastereoselectivity. Loss of aldolase activity; when associated with Q-73 and F-209.
- F131 (≠ P136) Plays a key role in the stabilization of the transition state and positioning the aldehyde component; mutation to A: Has a slight preference for the D-aldehyde and shows an inversion of the diastereoselectivity. Loss of aldolase activity; when associated with W-206.
- H155 (≠ L160) binding
- F206 (= F208) mutation to W: Decrease of aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P). Loss of aldolase activity; when associated with A-131.
Sites not aligning to the query:
- 207:215 mutation Missing: Loss of aldolase activity. Has a slight preference for the D-aldehyde.
- 209 Plays a key role in the stabilization of the transition state and positioning the aldehyde component; Y→F: Slowly inactivated and unable to discriminate between the enantiomers. Shows an inversion of the diastereoselectivity. Loss of aldolase activity; when associated with Q-73 and F-113.
- 211:215 mutation Missing: Decrease of aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).
2fuaA L-fuculose 1-phosphate aldolase crystal form t with cobalt (see paper)
30% identity, 96% coverage: 7:209/212 of query aligns to 6:207/210 of 2fuaA
Sites not aligning to the query:
1dzuP L-fuculose-1-phosphate aldolase from escherichia coli mutant t26a (see paper)
30% identity, 96% coverage: 7:209/212 of query aligns to 6:207/209 of 1dzuP
4fuaA L-fuculose-1-phosphate aldolase complex with pgh (see paper)
29% identity, 95% coverage: 7:208/212 of query aligns to 6:206/206 of 4fuaA
- active site: E73 (≠ T74), H92 (= H93), H94 (= H95), Y113 (= Y120), A117 (≠ K124), H155 (≠ L160)
- binding phosphoglycolohydroxamic acid: G28 (= G29), N29 (= N30), T43 (= T44), S71 (= S72), S72 (≠ K73), E73 (≠ T74), H92 (= H93), H94 (= H95), H155 (≠ L160)
- binding zinc ion: H92 (= H93), H94 (= H95), H155 (≠ L160)
7x78A L-fuculose 1-phosphate aldolase (see paper)
32% identity, 86% coverage: 27:208/212 of query aligns to 23:203/203 of 7x78A
Sites not aligning to the query:
P0DTQ0 5-deoxy-D-ribulose 1-phosphate aldolase; 5-deoxyribose disposal aldolase; EC 4.1.2.- from Bacillus thuringiensis serovar kurstaki (strain ATCC 35866 / NRRL B-4488 / HD73) (see paper)
26% identity, 96% coverage: 8:210/212 of query aligns to 7:209/213 of P0DTQ0
- E76 (≠ T74) binding
- H95 (= H93) binding
- H97 (= H95) binding
- H157 (≠ L160) binding
6btgA Crystal structure of deoxyribose-phosphate aldolase bound with dhap from bacillus thuringiensis (see paper)
27% identity, 95% coverage: 8:208/212 of query aligns to 7:207/207 of 6btgA
4c25A L-fuculose 1-phosphate aldolase (see paper)
25% identity, 97% coverage: 5:209/212 of query aligns to 7:211/212 of 4c25A
1jdiA Crystal structure of l-ribulose-5-phosphate 4-epimerase (see paper)
23% identity, 87% coverage: 7:190/212 of query aligns to 5:201/223 of 1jdiA
P08203 L-ribulose-5-phosphate 4-epimerase AraD; Phosphoribulose isomerase; EC 5.1.3.4 from Escherichia coli (strain K12) (see 4 papers)
23% identity, 87% coverage: 7:190/212 of query aligns to 5:201/231 of P08203
- N28 (= N30) mutation to A: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P).
- K42 (≠ T42) mutation to M: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P).
- D76 (≠ T74) mutation to N: Mutant shows a strong decrease of the catalytic efficiency, but it retains considerable epimerase activity. The affinity for L-ribulose 5-phosphate (LRu5P) is relatively unaffected.
- H95 (= H93) binding ; mutation to N: Mutant shows a strong decrease of the catalytic efficiency and a reduced affinity for Zn(2+).
- H97 (= H95) binding ; mutation to N: Mutant shows a strong decrease of the catalytic efficiency and a reduced affinity for Zn(2+). Inhibited by glycolaldehyde phosphate.
- T116 (vs. gap) mutation T->E,Y: Loss of the epimerase activity due to an increased steric bulk introduced by the mutation which causes a conformational change that is incompatible with catalysis.
- D120 (vs. gap) mutation to N: Loss of the epimerase activity.
- E142 (≠ V122) mutation to Q: Mutant shows a strong decrease of the catalytic efficiency, but it retains considerable epimerase activity. The affinity for L-ribulose 5-phosphate (LRu5P) is relatively unaffected.
- H171 (≠ L160) binding
Sites not aligning to the query:
- 218 H→N: Mutant shows a strong decrease of the catalytic efficiency, but it retains considerable epimerase activity. The affinity for L-ribulose 5-phosphate (LRu5P) is relatively unaffected.
- 229 Y→F: Loss of the epimerase activity.
Query Sequence
>RR42_RS10970 FitnessBrowser__Cup4G11:RR42_RS10970
MSTEASLREEICRIGASLYQRGYTVGSAGNISARMEDGWLITPTDACLGMLDPAAIAKVD
SGGNWVAGDKPSKTLTLHRAVYDNNPQAHGVVHTHSTHLVALSLAGAWRPDDVLPPITPY
YVMKVGHIPLIPYHRPGDPAVAARVAQLAAEVRGVLLARLGPVVWEATVSRAAFALEELE
ETARLWLMLKDKPDPLDEQALAELRDTFKARW
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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