SitesBLAST
Comparing WP_058932579.1 NCBI__GCF_001484605.1:WP_058932579.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 16 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)
38% identity, 94% coverage: 15:234/234 of query aligns to 5:231/231 of P08203
- N28 (= N38) mutation to A: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P).
- K42 (= K52) mutation to M: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P).
- D76 (= D94) 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 (= H113) binding Zn(2+); mutation to N: Mutant shows a strong decrease of the catalytic efficiency and a reduced affinity for Zn(2+).
- H97 (= H115) 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 (= T134) 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 (= D138) 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 (= H178) binding Zn(2+)
- H218 (≠ L224) 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 (= Y232) mutation to F: Loss of the epimerase activity.
1jdiA Crystal structure of l-ribulose-5-phosphate 4-epimerase (see paper)
38% identity, 91% coverage: 15:227/234 of query aligns to 5:221/223 of 1jdiA
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)
32% identity, 87% coverage: 14:216/234 of query aligns to 5:193/215 of P0AB87
- T26 (= T35) 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 substrate
- 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 (≠ SG 54:55) binding substrate
- S71 (= S92) mutation to A: Loss of aldolase activity; when associated with L-29.; mutation to Q: Loss of aldolase activity.
- SS 71:72 (= SS 92:93) binding substrate
- E73 (≠ D94) 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 (= H113) binding Zn(2+)
- H94 (= H115) binding Zn(2+)
- Y113 (≠ T134) 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 (≠ I152) 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 (= H178) 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).
4fuaA L-fuculose-1-phosphate aldolase complex with pgh (see paper)
32% identity, 87% coverage: 14:216/234 of query aligns to 5:193/206 of 4fuaA
- active site: E73 (≠ D94), H92 (= H113), H94 (= H115), Y113 (≠ T134), A117 (≠ D138), H155 (= H178)
- binding phosphoglycolohydroxamic acid: G28 (= G37), N29 (= N38), T43 (≠ S54), S71 (= S92), S72 (= S93), E73 (≠ D94), H92 (= H113), H94 (= H115), H155 (= H178)
- binding zinc ion: H92 (= H113), H94 (= H115), H155 (= H178)
2fuaA L-fuculose 1-phosphate aldolase crystal form t with cobalt (see paper)
32% identity, 87% coverage: 14:216/234 of query aligns to 5:193/210 of 2fuaA
Sites not aligning to the query:
1dzuP L-fuculose-1-phosphate aldolase from escherichia coli mutant t26a (see paper)
31% identity, 87% coverage: 14:216/234 of query aligns to 5:193/209 of 1dzuP
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: 12:234/234 of query aligns to 3:212/213 of P0DTQ0
- E76 (≠ D94) binding Mn(2+)
- H95 (= H113) binding Mn(2+)
- H97 (= H115) binding Mn(2+)
- H157 (= H178) binding Mn(2+)
6btgA Crystal structure of deoxyribose-phosphate aldolase bound with dhap from bacillus thuringiensis (see paper)
27% identity, 93% coverage: 12:228/234 of query aligns to 3:207/207 of 6btgA
7x78A L-fuculose 1-phosphate aldolase (see paper)
31% identity, 87% coverage: 14:216/234 of query aligns to 5:190/203 of 7x78A
- binding magnesium ion: E70 (≠ D94), H89 (= H113), H91 (= H115), H152 (= H178)
- binding sulfate ion: R5 (= R14), R8 (= R17), N26 (= N38), T40 (≠ S54), H61 (≠ G82), Q63 (≠ W84), S68 (= S92), S69 (= S93)
4c25A L-fuculose 1-phosphate aldolase (see paper)
24% identity, 92% coverage: 15:229/234 of query aligns to 9:211/212 of 4c25A
6voqA Crystal structure of ygbl, a putative aldolase/epimerase/decarboxylase from klebsiella pneumoniae
29% identity, 83% coverage: 11:204/234 of query aligns to 3:187/207 of 6voqA
4xxfA L-fuculose 1-phosphate aldolase from glaciozyma antarctica pi12 (see paper)
24% identity, 78% coverage: 36:218/234 of query aligns to 43:212/249 of 4xxfA
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)
25% identity, 81% coverage: 16:204/234 of query aligns to 3:174/181 of Q58813
- N25 (= N38) 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.
8il8A Crystal structure of pyruvic oxime dioxygenase (pod) from alcaligenes faecalis
29% identity, 71% coverage: 36:202/234 of query aligns to 23:179/230 of 8il8A
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)
27% identity, 81% coverage: 35:223/234 of query aligns to 24:208/234 of Q988D0
- E73 (≠ D94) binding Mn(2+)
- H92 (= H113) binding Mn(2+)
- H94 (= H115) binding Mn(2+)
- H163 (= H178) binding Mn(2+)
2z7bA Crystal structure of mesorhizobium loti 3-hydroxy-2-methylpyridine-4, 5-dicarboxylate decarboxylase (see paper)
27% identity, 81% coverage: 35:223/234 of query aligns to 27:211/237 of 2z7bA
Query Sequence
>WP_058932579.1 NCBI__GCF_001484605.1:WP_058932579.1
MSTATAKTLDTIARIRREVCALHAELTRYGLVVWTAGNVSARVPGRDLMVIKPSGVSYED
LTPEQMVVTDLYGVAVDGDADGEWGNPPLSPSSDTAAHAYVYRHMPDVGGVVHTHSTYAT
AWAARGESIPCVLTMMGDEFGGSIPVGPFALIGDDSIGQGIVETLKNSTSPAVLMQNHGP
FTIGKDARSAVKAAVMCEEVARTVHISRQLGEPITIDQGHIDSLYARYQNVYGQ
Or try a new SitesBLAST search
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