SitesBLAST
Comparing WP_084932211.1 NCBI__GCF_002095475.1:WP_084932211.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 14 hits to proteins with known functional sites (download)
6voqA Crystal structure of ygbl, a putative aldolase/epimerase/decarboxylase from klebsiella pneumoniae
44% identity, 86% coverage: 4:185/212 of query aligns to 4:186/207 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)
33% identity, 86% coverage: 8:189/212 of query aligns to 3:176/181 of Q58813
- N25 (= N30) mutation to L: It shows a 3-fold increase of the affinity 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 affinity for dihydroxyacetone phosphate (DHAP), but has the same affinity for DL-glyceraldehyde compared to the wild-type.
1dzuP L-fuculose-1-phosphate aldolase from escherichia coli mutant t26a (see paper)
26% identity, 87% coverage: 5:189/212 of query aligns to 4:184/209 of 1dzuP
4fuaA L-fuculose-1-phosphate aldolase complex with pgh (see paper)
26% identity, 87% coverage: 5:189/212 of query aligns to 4:184/206 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)
2fuaA L-fuculose 1-phosphate aldolase crystal form t with cobalt (see paper)
26% identity, 87% coverage: 5:189/212 of query aligns to 4:184/210 of 2fuaA
Sites not aligning to the query:
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)
26% identity, 87% coverage: 5:189/212 of query aligns to 4:184/215 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 (≠ S28) mutation Missing: Strong decrease of the aldolase activity.
- GN 28:29 (= GN 29:30) binding substrate
- 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 substrate
- 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 substrate
- E73 (≠ T74) active site, Proton donor/acceptor; binding Zn(2+); 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 Zn(2+)
- H94 (= H95) binding Zn(2+)
- 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 Zn(2+)
Sites not aligning to the query:
- 206 F→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 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).
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)
27% identity, 95% coverage: 8:209/212 of query aligns to 7:208/213 of P0DTQ0
- E76 (≠ T74) binding Mn(2+)
- H95 (= H93) binding Mn(2+)
- H97 (= H95) binding Mn(2+)
- H157 (≠ L160) binding Mn(2+)
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
7x78A L-fuculose 1-phosphate aldolase (see paper)
26% identity, 87% coverage: 5:189/212 of query aligns to 4:181/203 of 7x78A
- binding magnesium ion: E70 (≠ T74), H89 (= H93), H91 (= H95), H152 (≠ L160)
- binding sulfate ion: R5 (≠ T6), R8 (≠ E9), N26 (= N30), T40 (= T44), H61 (≠ W65), Q63 (≠ N67), S68 (= S72), S69 (≠ K73)
4c25A L-fuculose 1-phosphate aldolase (see paper)
23% identity, 91% coverage: 7:199/212 of query aligns to 9:199/212 of 4c25A
1jdiA Crystal structure of l-ribulose-5-phosphate 4-epimerase (see paper)
25% identity, 86% coverage: 7:188/212 of query aligns to 5:199/223 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)
25% identity, 86% coverage: 7:188/212 of query aligns to 5:199/231 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 Zn(2+); mutation to N: Mutant shows a strong decrease of the catalytic efficiency and a reduced affinity for Zn(2+).
- H97 (= H95) binding Zn(2+); mutation to N: Mutant shows a strong decrease of the catalytic efficiency and a reduced affinity for Zn(2+). Inhibited by glycolaldehyde phosphate.
- T116 (= T118) 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 (≠ V122) 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 (≠ L160) binding Zn(2+)
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.
4m6rA Structural and biochemical basis for the inhibition of cell death by apip, a methionine salvage enzyme (see paper)
24% identity, 83% coverage: 3:177/212 of query aligns to 5:194/224 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)
24% identity, 83% coverage: 3:177/212 of query aligns to 23:212/242 of Q96GX9
- H23 (= H3) to R: in dbSNP:rs17850326
- C76 (≠ V59) to Y: in dbSNP:rs1977420
- S84 (≠ N67) 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 (≠ K70) 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 (= S72) 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 (≠ R79) mutation to A: Mildly reduced enzyme activity.
- C97 (≠ T80) 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 (= H93) 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 (= H95) 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 (≠ G126) 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 (vs. gap) to V: in dbSNP:rs17850327
- H195 (≠ L160) 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
Query Sequence
>WP_084932211.1 NCBI__GCF_002095475.1:WP_084932211.1
MSHENTIREEICQTGHSLHRRGYTVGSSGNISAKLEDGWLITPTDVCLGSLRPDMIAKVN
LEGEWVNGGKPSKTLKLHRTIYENNDAVRGIVHTHSTHLVAMTLGEVWSKESILPPITPY
QVMKVGRIPLISYCRPGSPDVAVQAGELAHDVKGIMLERLGPVIWGTSVTKAAEILEELE
ETAKLWLMTHPKPESLSQPALQDLFDTFDCRW
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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