SitesBLAST
Comparing H281DRAFT_01508 FitnessBrowser__Burk376:H281DRAFT_01508 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
45% identity, 92% coverage: 12:213/220 of query aligns to 4:207/207 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)
34% identity, 82% coverage: 18:197/220 of query aligns to 8:176/181 of Q58813
- N25 (= N38) 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)
27% identity, 94% coverage: 14:219/220 of query aligns to 5:212/215 of P0AB87
- T26 (≠ S35) mutation to A: Decrease of the aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).
- A27 (= A36) mutation Missing: Strong decrease of the aldolase activity.
- GN 28:29 (= GN 37:38) binding
- N29 (= N38) 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 52:53) binding
- S71 (= S80) mutation to A: Loss of aldolase activity; when associated with L-29.; mutation to Q: Loss of aldolase activity.
- SS 71:72 (≠ SK 80:81) binding
- E73 (≠ T82) 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 (= H101) binding
- H94 (= H103) binding
- Y113 (= Y128) 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 (≠ P144) 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 (≠ L168) binding
- F206 (≠ L212) 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 (≠ F216) 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).
4fuaA L-fuculose-1-phosphate aldolase complex with pgh (see paper)
27% identity, 88% coverage: 14:206/220 of query aligns to 5:197/206 of 4fuaA
- active site: E73 (≠ T82), H92 (= H101), H94 (= H103), Y113 (= Y128), A117 (≠ K132), H155 (≠ L168)
- binding phosphoglycolohydroxamic acid: G28 (= G37), N29 (= N38), T43 (= T52), S71 (= S80), S72 (≠ K81), E73 (≠ T82), H92 (= H101), H94 (= H103), H155 (≠ L168)
- binding zinc ion: H92 (= H101), H94 (= H103), H155 (≠ L168)
2fuaA L-fuculose 1-phosphate aldolase crystal form t with cobalt (see paper)
27% identity, 88% coverage: 14:206/220 of query aligns to 5:197/210 of 2fuaA
Sites not aligning to the query:
1dzuP L-fuculose-1-phosphate aldolase from escherichia coli mutant t26a (see paper)
27% identity, 88% coverage: 14:206/220 of query aligns to 5:197/209 of 1dzuP
7x78A L-fuculose 1-phosphate aldolase (see paper)
28% identity, 79% coverage: 35:207/220 of query aligns to 23:195/203 of 7x78A
Sites not aligning to the query:
6btgA Crystal structure of deoxyribose-phosphate aldolase bound with dhap from bacillus thuringiensis (see paper)
30% identity, 92% coverage: 14:216/220 of query aligns to 5:207/207 of 6btgA
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)
30% identity, 92% coverage: 14:216/220 of query aligns to 5:207/213 of P0DTQ0
- E76 (≠ T82) binding
- H95 (= H101) binding
- H97 (= H103) binding
- H157 (≠ L168) binding
4c25A L-fuculose 1-phosphate aldolase (see paper)
26% identity, 92% coverage: 15:216/220 of query aligns to 9:210/212 of 4c25A
4m6rA Structural and biochemical basis for the inhibition of cell death by apip, a methionine salvage enzyme (see paper)
31% identity, 43% coverage: 18:112/220 of query aligns to 12:108/224 of 4m6rA
Sites not aligning to the query:
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)
31% identity, 43% coverage: 18:112/220 of query aligns to 30:126/242 of Q96GX9
- C76 (≠ V67) to Y: in dbSNP:rs1977420
- S84 (= S75) 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 (≠ K78) 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 (= S80) 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 (vs. gap) mutation to A: Mildly reduced enzyme activity.
- C97 (vs. gap) 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 (= H101) 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 (= H103) 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.
Sites not aligning to the query:
- 7 R → W: in dbSNP:rs2956114
- 23 H → R: in dbSNP:rs17850326
- 139 active site, Proton donor/acceptor; E→A: Almost complete loss of enzyme activity. Abolishes protection against pyroptosis. No effect on anti-apoptotic activity.
- 181 M → V: in dbSNP:rs17850327
- 195 H→A: Impaired ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with 87-A--A-89.
Query Sequence
>H281DRAFT_01508 FitnessBrowser__Burk376:H281DRAFT_01508
MSNAPAVHATNEARVREEICVTGASLYQRGYTVGSAGNISARLDDGWLITPTDACLGRLD
PTDIAKVDFDGNAVSGGKPSKTLALHRGIYARNGETRGIVHTHSTHLVALTLAGVWSEAD
VLPPITPYYVMKVGHVPLIRYRRPGDPQVAAQIAALADSVRAVLLERLGPVVWERSVAHA
SYALEELEETARLWLMTNPRPAPLDEASLEELRSAFGARW
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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