SitesBLAST
Comparing WP_012968949.1 NCBI__GCF_000025465.1:WP_012968949.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 13 hits to proteins with known functional sites (download)
P08203 L-ribulose-5-phosphate 4-epimerase AraD; Phosphoribulose isomerase; EC 5.1.3.4 from Escherichia coli (strain K12) (see 4 papers)
93% identity, 100% coverage: 1:231/231 of query aligns to 1:231/231 of P08203
- N28 (= N28) mutation to A: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P).
- K42 (= K42) mutation to M: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P).
- D76 (= D76) 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 Zn(2+); mutation to N: Mutant shows a strong decrease of the catalytic efficiency and a reduced affinity for Zn(2+).
- H97 (= H97) 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 (= T116) 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 (= D120) mutation to N: Loss of the epimerase activity.
- E142 (= E142) 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 (= H171) binding Zn(2+)
- H218 (= H218) 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.
- Y229 (= Y229) mutation to F: Loss of the epimerase activity.
1jdiA Crystal structure of l-ribulose-5-phosphate 4-epimerase (see paper)
92% identity, 97% coverage: 1:223/231 of query aligns to 1:223/223 of 1jdiA
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)
29% identity, 100% coverage: 1:231/231 of query aligns to 2:212/213 of P0DTQ0
- E76 (≠ D76) binding Mn(2+)
- H95 (= H95) binding Mn(2+)
- H97 (= H97) binding Mn(2+)
- H157 (= H171) binding Mn(2+)
6btgA Crystal structure of deoxyribose-phosphate aldolase bound with dhap from bacillus thuringiensis (see paper)
30% identity, 89% coverage: 1:206/231 of query aligns to 2:185/207 of 6btgA
4c25A L-fuculose 1-phosphate aldolase (see paper)
33% identity, 48% coverage: 4:114/231 of query aligns to 8:117/212 of 4c25A
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)
33% identity, 54% coverage: 5:128/231 of query aligns to 6:125/215 of P0AB87
- T26 (= T25) mutation to A: Decrease of the aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).
- A27 (≠ W26) mutation Missing: Strong decrease of the aldolase activity.
- GN 28:29 (= GN 27:28) binding substrate
- N29 (= N28) 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 (≠ SG 44:45) binding substrate
- S71 (= S74) mutation to A: Loss of aldolase activity; when associated with L-29.; mutation to Q: Loss of aldolase activity.
- SS 71:72 (= SS 74:75) binding substrate
- E73 (≠ D76) 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 (= H95) binding Zn(2+)
- H94 (= H97) binding Zn(2+)
- Y113 (≠ T116) 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.
Sites not aligning to the query:
- 131 Plays a key role in the stabilization of the transition state and positioning the aldehyde component; F→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.
- 155 binding Zn(2+)
- 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).
4fuaA L-fuculose-1-phosphate aldolase complex with pgh (see paper)
33% identity, 54% coverage: 5:128/231 of query aligns to 6:125/206 of 4fuaA
- active site: E73 (≠ D76), H92 (= H95), H94 (= H97), Y113 (≠ T116), A117 (≠ D120)
- binding phosphoglycolohydroxamic acid: G28 (= G27), N29 (= N28), T43 (≠ S44), S71 (= S74), S72 (= S75), E73 (≠ D76), H92 (= H95), H94 (= H97)
- binding zinc ion: H92 (= H95), H94 (= H97)
Sites not aligning to the query:
2fuaA L-fuculose 1-phosphate aldolase crystal form t with cobalt (see paper)
33% identity, 54% coverage: 5:128/231 of query aligns to 6:125/210 of 2fuaA
Sites not aligning to the query:
7x78A L-fuculose 1-phosphate aldolase (see paper)
31% identity, 54% coverage: 5:128/231 of query aligns to 6:122/203 of 7x78A
Sites not aligning to the query:
1dzuP L-fuculose-1-phosphate aldolase from escherichia coli mutant t26a (see paper)
32% identity, 54% coverage: 5:128/231 of query aligns to 6:125/209 of 1dzuP
Sites not aligning to the query:
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)
24% identity, 84% coverage: 6:199/231 of query aligns to 3:175/181 of Q58813
- N25 (= N28) 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.
6voqA Crystal structure of ygbl, a putative aldolase/epimerase/decarboxylase from klebsiella pneumoniae
26% identity, 84% coverage: 3:196/231 of query aligns to 5:186/207 of 6voqA
4xxfA L-fuculose 1-phosphate aldolase from glaciozyma antarctica pi12 (see paper)
25% identity, 66% coverage: 41:192/231 of query aligns to 59:193/249 of 4xxfA
Query Sequence
>WP_012968949.1 NCBI__GCF_000025465.1:WP_012968949.1
MLEDLKRQVLEANLALPQHNLVTLTWGNVSAVDRDQGVLVIKPSGVDYRVMTADDMVVVS
LETGEVVEGNKKPSSDTPTHRLLYQAFPTLGGIVHTHSRHATIWAQAGQSIPATGTTHAD
YFYGPVPCTRLMTDAEINGEYEWETGNVIVETFRQQGIDPAQMPGVLVHSHGPFAWGKNA
EDAVHNAIVLEEIAYMGIFCRQLAPQLPDMQQTLLDKHYLRKHGAKAYYGQ
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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