SitesBLAST
Comparing SMc01621 FitnessBrowser__Smeli:SMc01621 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)
47% identity, 95% coverage: 1:212/222 of query aligns to 1:210/215 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 (≠ S27) 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 (≠ SA 43:44) binding
- S71 (= S74) mutation to A: Loss of aldolase activity; when associated with L-29.; mutation to Q: Loss of aldolase activity.
- SS 71:72 (≠ SV 74:75) binding
- E73 (= E76) 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 (= H95) binding
- H94 (= H97) binding
- Y113 (= Y116) 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 (≠ Y134) 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 (= H158) 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.
- Y209 (= Y211) 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.
Sites not aligning to the query:
- 207:215 mutation Missing: Loss of aldolase activity. Has a slight preference for the D-aldehyde.
- 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)
47% identity, 95% coverage: 1:212/222 of query aligns to 1:210/210 of 2fuaA
1dzuP L-fuculose-1-phosphate aldolase from escherichia coli mutant t26a (see paper)
46% identity, 95% coverage: 1:211/222 of query aligns to 1:209/209 of 1dzuP
4fuaA L-fuculose-1-phosphate aldolase complex with pgh (see paper)
46% identity, 94% coverage: 1:208/222 of query aligns to 1:206/206 of 4fuaA
- active site: E73 (= E76), H92 (= H95), H94 (= H97), Y113 (= Y116), A117 (= A120), H155 (= H158)
- binding phosphoglycolohydroxamic acid: G28 (= G28), N29 (= N29), T43 (≠ S43), S71 (= S74), S72 (≠ V75), E73 (= E76), H92 (= H95), H94 (= H97), H155 (= H158)
- binding zinc ion: H92 (= H95), H94 (= H97), H155 (= H158)
7x78A L-fuculose 1-phosphate aldolase (see paper)
46% identity, 94% coverage: 1:208/222 of query aligns to 1:203/203 of 7x78A
- binding magnesium ion: E70 (= E76), H89 (= H95), H91 (= H97), H152 (= H158)
- binding sulfate ion: R5 (≠ Q5), R8 (≠ Q8), N26 (= N29), T40 (≠ S43), H61 (≠ Y64), Q63 (≠ A66), S68 (= S74), S69 (≠ V75)
4c25A L-fuculose 1-phosphate aldolase (see paper)
43% identity, 92% coverage: 5:208/222 of query aligns to 8:210/212 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)
38% identity, 94% coverage: 7:214/222 of query aligns to 7:213/213 of P0DTQ0
- E76 (= E76) binding
- H95 (= H95) binding
- H97 (= H97) binding
- H157 (= H158) binding
6btgA Crystal structure of deoxyribose-phosphate aldolase bound with dhap from bacillus thuringiensis (see paper)
38% identity, 91% coverage: 7:208/222 of query aligns to 7:207/207 of 6btgA
6voqA Crystal structure of ygbl, a putative aldolase/epimerase/decarboxylase from klebsiella pneumoniae
30% identity, 83% coverage: 1:185/222 of query aligns to 2:188/207 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)
29% identity, 79% coverage: 7:182/222 of query aligns to 3:171/181 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.
P08203 L-ribulose-5-phosphate 4-epimerase AraD; Phosphoribulose isomerase; EC 5.1.3.4 from Escherichia coli (strain K12) (see 4 papers)
33% identity, 70% coverage: 26:181/222 of query aligns to 25:194/231 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 (≠ E76) 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 (= H95) binding ; mutation to N: Mutant shows a strong decrease of the catalytic efficiency and a reduced affinity for Zn(2+).
- H97 (= H97) 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 (≠ Y116) 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 (≠ A120) mutation to N: Loss of the epimerase activity.
- E142 (≠ A132) 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 (= H158) 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.
1jdiA Crystal structure of l-ribulose-5-phosphate 4-epimerase (see paper)
33% identity, 70% coverage: 26:181/222 of query aligns to 25:194/223 of 1jdiA
2z7bA Crystal structure of mesorhizobium loti 3-hydroxy-2-methylpyridine-4, 5-dicarboxylate decarboxylase (see paper)
26% identity, 89% coverage: 4:201/222 of query aligns to 2:209/237 of 2z7bA
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)
26% identity, 88% coverage: 6:201/222 of query aligns to 1:206/234 of Q988D0
- E73 (= E76) binding
- H92 (= H95) binding
- H94 (= H97) binding
- H163 (= H158) binding
4xxfA L-fuculose 1-phosphate aldolase from glaciozyma antarctica pi12 (see paper)
22% identity, 78% coverage: 6:178/222 of query aligns to 22:192/249 of 4xxfA
4m6rA Structural and biochemical basis for the inhibition of cell death by apip, a methionine salvage enzyme (see paper)
28% identity, 77% coverage: 1:170/222 of query aligns to 1:189/224 of 4m6rA
Q96GX9 Methylthioribulose-1-phosphate dehydratase; MTRu-1-P dehydratase; APAF1-interacting protein; hAPIP; EC 4.2.1.109 from Homo sapiens (Human) (see 5 papers)
28% identity, 74% coverage: 7:170/222 of query aligns to 25:207/242 of Q96GX9
- C76 (≠ A57) to Y: in dbSNP:rs1977420
- S84 (≠ G65) mutation S->A,D: Does not affect ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A,D-87 and A,D-89.
- S87 (≠ V68) mutation S->A,D: Does not affect ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A,D-84 and A,D-89.
- S89 (≠ P70) mutation S->A,D: Does not affect ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A,D-84 and A,D-87.
- Q96 (≠ V75) mutation to A: Mildly reduced enzyme activity.
- C97 (≠ E76) mutation to A: Acts as a dominant negative mutant; unable to use 5'-methylthioadenosine as source of methionine. Does not affect the ability to bind CASP1 and to inhibit cell death induced by CASP9 overexpression.; mutation to A: Almost complete loss of enzyme activity. Abolishes protection against pyroptosis. No effect on anti-apoptotic activity.
- H115 (= H95) mutation to A: Almost complete loss of enzyme activity. Abolishes protection against pyroptosis. No effect on anti-apoptotic activity.; mutation to A: Impaired ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A-117 and A-195. Unable to inhibit both CASP1 and CASP9 mediated cell death.
- H117 (= H97) mutation to A: Impaired ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A-115 and A-195.
- E139 (≠ Y116) active site, Proton donor/acceptor; mutation to A: Almost complete loss of enzyme activity. Abolishes protection against pyroptosis. No effect on anti-apoptotic activity.
- M181 (= M147) to V: in dbSNP:rs17850327
- H195 (= H158) mutation to A: Impaired ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with 87-A--A-89.
Sites not aligning to the query:
- 7 R → W: in dbSNP:rs2956114
- 23 H → R: in dbSNP:rs17850326
P35612 Beta-adducin; Erythrocyte adducin subunit beta from Homo sapiens (Human) (see 2 papers)
24% identity, 97% coverage: 3:218/222 of query aligns to 130:359/726 of P35612
Sites not aligning to the query:
- 55 modified: Phosphothreonine; by PKA
- 439 T → A: in dbSNP:rs17855969
- 703 modified: Phosphoserine; by PKC
- 713 modified: Phosphoserine; by PKA and PKC
Query Sequence
>SMc01621 FitnessBrowser__Smeli:SMc01621
MNELQLRQSIIDHCRHMNAIGLNQGTSGNISLRHGGTMLITPSAIPYAEMTPDMIVAMPI
EGEYGAWVGPKKPSVEWPFHLDILRARPDVGAVVHTHASFSTILAMARKPIPACHYMIAA
FGGSDVRVADYARYGTKALSENVLKAMEGRSACLMANHGMIATGSSLEKAMWAAVELETI
AKQYYHVLLIGGPVVLPQEEIAGVIEGFATYGHQDKPKGEAA
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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