SitesBLAST
Comparing BWI76_RS22915 FitnessBrowser__Koxy:BWI76_RS22915 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 18 hits to proteins with known functional sites (download)
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)
92% identity, 100% coverage: 1:215/215 of query aligns to 1:215/215 of P0AB87
- T26 (= T26) mutation to A: Decrease of the aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).
- A27 (= A27) mutation Missing: Strong decrease of the aldolase activity.
- GN 28:29 (= GN 28:29) binding
- N29 (= N29) 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 (= TG 43:44) binding
- S71 (= S71) mutation to A: Loss of aldolase activity; when associated with L-29.; mutation to Q: Loss of aldolase activity.
- SS 71:72 (= SS 71:72) binding
- E73 (= E73) 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 (= H92) binding
- H94 (= H94) binding
- Y113 (= Y113) 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 (= F131) 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 (= H155) binding
- F206 (= F206) 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.
- 207:215 (vs. 207:215, 100% identical) mutation Missing: Loss of aldolase activity. Has a slight preference for the D-aldehyde.
- Y209 (= Y209) Plays a key role in the stabilization of the transition state and positioning the aldehyde component; mutation to 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.
- LRIEE 211:215 (= LRIEE 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)
91% identity, 98% coverage: 1:210/215 of query aligns to 1:210/210 of 2fuaA
1dzuP L-fuculose-1-phosphate aldolase from escherichia coli mutant t26a (see paper)
91% identity, 97% coverage: 1:209/215 of query aligns to 1:209/209 of 1dzuP
4fuaA L-fuculose-1-phosphate aldolase complex with pgh (see paper)
91% identity, 96% coverage: 1:206/215 of query aligns to 1:206/206 of 4fuaA
- active site: E73 (= E73), H92 (= H92), H94 (= H94), Y113 (= Y113), A117 (= A117), H155 (= H155)
- binding phosphoglycolohydroxamic acid: G28 (= G28), N29 (= N29), T43 (= T43), S71 (= S71), S72 (= S72), E73 (= E73), H92 (= H92), H94 (= H94), H155 (= H155)
- binding zinc ion: H92 (= H92), H94 (= H94), H155 (= H155)
7x78A L-fuculose 1-phosphate aldolase (see paper)
93% identity, 96% coverage: 1:206/215 of query aligns to 1:203/203 of 7x78A
- binding magnesium ion: E70 (= E73), H89 (= H92), H91 (= H94), H152 (= H155)
- binding sulfate ion: R5 (= R5), R8 (= R8), N26 (= N29), T40 (= T43), H61 (= H64), Q63 (= Q66), S68 (= S71), S69 (= S72)
4c25A L-fuculose 1-phosphate aldolase (see paper)
40% identity, 96% coverage: 1:207/215 of query aligns to 4:211/212 of 4c25A
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)
37% identity, 94% coverage: 9:210/215 of query aligns to 9:211/213 of P0DTQ0
- E76 (= E73) binding
- H95 (= H92) binding
- H97 (= H94) binding
- H157 (= H155) binding
6btgA Crystal structure of deoxyribose-phosphate aldolase bound with dhap from bacillus thuringiensis (see paper)
38% identity, 88% coverage: 9:197/215 of query aligns to 9:199/207 of 6btgA
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)
28% identity, 84% coverage: 8:187/215 of query aligns to 4:179/181 of Q58813
- N25 (= N29) 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.
6voqA Crystal structure of ygbl, a putative aldolase/epimerase/decarboxylase from klebsiella pneumoniae
28% identity, 85% coverage: 1:183/215 of query aligns to 2:189/207 of 6voqA
4xxfA L-fuculose 1-phosphate aldolase from glaciozyma antarctica pi12 (see paper)
24% identity, 88% coverage: 2:190/215 of query aligns to 18:213/249 of 4xxfA
1jdiA Crystal structure of l-ribulose-5-phosphate 4-epimerase (see paper)
28% identity, 76% coverage: 6:168/215 of query aligns to 5:184/223 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)
28% identity, 76% coverage: 6:168/215 of query aligns to 5:184/231 of P08203
- N28 (= N29) mutation to A: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P).
- K42 (≠ T41) mutation to M: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P).
- D76 (≠ E73) 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 (= H92) binding ; mutation to N: Mutant shows a strong decrease of the catalytic efficiency and a reduced affinity for Zn(2+).
- H97 (= H94) 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 (≠ Y113) 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 (≠ A117) mutation to N: Loss of the epimerase activity.
- E142 (vs. gap) 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 (= H155) 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.
P35611 Alpha-adducin; Erythrocyte adducin subunit alpha from Homo sapiens (Human) (see 5 papers)
27% identity, 71% coverage: 35:186/215 of query aligns to 177:333/737 of P35611
Sites not aligning to the query:
- 59 modified: Phosphoserine; by PKA
- 408 modified: Phosphoserine; by PKA
- 436 modified: Phosphoserine; by PKA
- 445 modified: Phosphothreonine; by ROCK2; T→D: Abolishes phosphorylation by ROCK2; when associated with D-480.
- 460 G → W: in dbSNP:rs4961
- 480 modified: Phosphothreonine; by ROCK2; T→D: Abolishes phosphorylation by ROCK2; when associated with D-445.
- 481 modified: Phosphoserine; by PKA
- 586 S → C: in dbSNP:rs4963
- 716 modified: Phosphoserine; by PKC
- 726 modified: Phosphoserine; by PKA and PKC
Q9QYB5 Gamma-adducin; Adducin-like protein 70 from Mus musculus (Mouse) (see paper)
27% identity, 84% coverage: 30:209/215 of query aligns to 161:344/706 of Q9QYB5
Sites not aligning to the query:
- 357 Cleavage by asparagine endopeptidase (AEP); N→A: Loss of cleavage by asparagine endopeptidase (AEP).
- 450 N→A: No effect on cleavage by asparagine endopeptidase (AEP).
- 457 N→A: No effect on cleavage by asparagine endopeptidase (AEP).
Q02645 Protein hu-li tai shao; Adducin-like protein from Drosophila melanogaster (Fruit fly) (see 2 papers)
23% identity, 87% coverage: 21:207/215 of query aligns to 134:328/1156 of Q02645
Sites not aligning to the query:
- 478 modified: Phosphoserine
- 480 modified: Phosphothreonine
- 498 modified: Phosphothreonine
- 603 modified: Phosphoserine
- 608 modified: Phosphotyrosine
- 609 modified: Phosphothreonine
- 611 modified: Phosphothreonine
- 614 modified: Phosphoserine
- 627 modified: Phosphotyrosine
- 630 modified: Phosphoserine
Q988D0 3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-decarboxylase; HMPDdc; EC 4.1.1.51 from Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099) (Mesorhizobium loti (strain MAFF 303099)) (see paper)
21% identity, 86% coverage: 6:190/215 of query aligns to 1:203/234 of Q988D0
- E73 (= E73) binding
- H92 (= H92) binding
- H94 (= H94) binding
- H163 (= H155) binding
2z7bA Crystal structure of mesorhizobium loti 3-hydroxy-2-methylpyridine-4, 5-dicarboxylate decarboxylase (see paper)
21% identity, 86% coverage: 6:190/215 of query aligns to 4:206/237 of 2z7bA
Query Sequence
>BWI76_RS22915 FitnessBrowser__Koxy:BWI76_RS22915
MERNRLARQIIDTCLEMTRLGLNQGTAGNVSVRYQGGMLITPTGIPYEKLTEAHIVYIDA
EGQHEQGKLPSSEWRFHLAAYQTRPDAHAVVHNHAVHCTAVSILNRPIPAIHYMIAAAGG
NSIPCAPYATFGTRELSEHVAVALKNRKATLLQHHGLIACEENLEKALWLAHEVEVLAQL
YLSTLAIIDPVPVLDDEAIAVVLEKFKTYGLRIEE
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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