SitesBLAST
Comparing WP_007734084.1 NCBI__GCF_002893965.1:WP_007734084.1 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 20 (the maximum) hits to proteins with known functional sites (download)
P9WMK5 4-hydroxy-2-oxohexanoate aldolase; 4-hydroxy-2-keto-pentanoic acid aldolase; 4-hydroxy-2-oxopentanoate aldolase; 4-hydroxy-2-oxovalerate aldolase; HOA; EC 4.1.3.43; EC 4.1.3.39 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
84% identity, 99% coverage: 1:343/347 of query aligns to 1:337/346 of P9WMK5
- D16 (= D22) binding Mn(2+)
- H198 (= H204) binding Mn(2+)
- H200 (= H206) binding Mn(2+)
- G322 (= G328) mutation to F: Abolishes substrate channeling to HsaG.
4jn6C Crystal structure of the aldolase-dehydrogenase complex from mycobacterium tuberculosis hrv37 (see paper)
86% identity, 96% coverage: 11:343/347 of query aligns to 2:334/339 of 4jn6C
- active site: D13 (= D22), H16 (= H25), H195 (= H204), H197 (= H206), Y286 (= Y295)
- binding manganese (ii) ion: D13 (= D22), H195 (= H204), H197 (= H206)
- binding oxalate ion: R12 (= R21), M136 (= M145), V164 (= V173), S166 (= S175), H195 (= H204), H197 (= H206), Y286 (= Y295)
4lrsA Crystal and solution structures of the bifunctional enzyme (aldolase/aldehyde dehydrogenase) from thermomonospora curvata, reveal a cofactor-binding domain motion during NAD+ and coa accommodation whithin the shared cofactor-binding site
63% identity, 95% coverage: 13:343/347 of query aligns to 4:334/337 of 4lrsA
- active site: D13 (= D22), H16 (= H25), H195 (= H204), H197 (= H206), Y286 (= Y295)
- binding magnesium ion: D13 (= D22), H195 (= H204), H197 (= H206)
- binding pyruvic acid: R12 (= R21), D13 (= D22), F134 (= F143), M136 (= M145), V164 (= V173), S166 (= S175), H195 (= H204), H197 (= H206), Y286 (= Y295)
Q53WI0 4-hydroxy-2-oxovalerate aldolase; HOA; 4-hydroxy-2-keto-pentanoic acid aldolase; 4-hydroxy-2-oxohexanoate aldolase; 4-hydroxy-2-oxopentanoate aldolase; EC 4.1.3.39; EC 4.1.3.43 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
52% identity, 97% coverage: 10:347/347 of query aligns to 2:344/347 of Q53WI0
- A324 (≠ G327) mutation to G: Increases the channeling efficiency of propanaldehyde from 57% to 94%.
8ih7A Amng-amnh complex
49% identity, 97% coverage: 7:342/347 of query aligns to 4:339/340 of 8ih7A
P51015 4-hydroxy-2-oxovalerate aldolase 4; HOA 4; 4-hydroxy-2-keto-pentanoic acid aldolase 4; 4-hydroxy-2-oxohexanoate aldolase; 4-hydroxy-2-oxopentanoate aldolase 4; EC 4.1.3.39; EC 4.1.3.43 from Paraburkholderia xenovorans (strain LB400) (see 3 papers)
50% identity, 95% coverage: 13:343/347 of query aligns to 8:338/346 of P51015
- R16 (= R21) mutation to A: Loss of aldol cleavage activity.; mutation to K: 4000-fold decrease in the catalytic efficiency of the aldol cleavage reaction.
- H20 (= H25) mutation H->A,S: 100-fold decrease in the catalytic efficiency of the aldol cleavage reaction. Dramatic reduction in acetaldehyde and propanaldehyde channeling efficiency by more than 70%.
- L87 (= L92) mutation to A: 32-fold reduction in the catalytic efficiency with acetaldehyde as substrate of the aldol addition reaction, but no change in the catalytic efficiency using propanaldehyde; thus, exhibits a 40-fold preference for propanaldehyde over acetaldehyde.; mutation L->N,W: Loss of aldolase activity (with either enantiomer of HOPA), but retains some decarboxylase activity for the smaller oxaloacetate substrate. In the retro-aldol cleavage reaction, is inactive toward 4(S)-HOPA but is active toward 4(R)-HOPA, albeit with a great reduction in catalytic efficiency, and in the aldol addition reaction, produces also exclusively the 4(R)-enantiomer; when associated with F-290.
- L89 (= L94) mutation to A: As the wild-type enzyme, exhibits similar catalytic efficiency with acetaldehyde or propanaldehyde as substrate in the aldol addition reaction but displays higher catalytic efficiency with longer aldehydes (50-fold increase using pentaldehyde). Shows a reduction in aldehyde channeling efficiency by 30%.
- Y290 (= Y295) mutation to F: Loss of stereochemical control as the mutant is able to catalyze the aldol cleavage of substrates with both R and S configurations at C4 with similar kinetic parameters. 3.5-fold decrease in the catalytic efficiency of the aldol cleavage reaction. Reduction in aldehyde channeling efficiency by more than 30%. In the retro-aldol cleavage reaction, is inactive toward 4(S)-HOPA but is active toward 4(R)-HOPA, albeit with a great reduction in catalytic efficiency, and in the aldol addition reaction, produces also exclusively the 4(R)-enantiomer; when associated with N-87 or W-87.; mutation to S: Loss of stereochemical control as the mutant is able to catalyze the aldol cleavage of substrates with both R and S configurations at C4 with similar kinetic parameters. 3.5-fold decrease in the catalytic efficiency of the aldol cleavage reaction.
- G322 (= G327) mutation to A: Displays a reduction in aldehyde channeling efficiency of about 20%.; mutation G->F,L: Unable to channel either acetaldehyde or propanaldehyde.
- G323 (= G328) mutation to A: Able to channel butyraldehyde (with less efficiency than wild-type) but not its isomer isobutyraldehyde.; mutation to F: Unable to channel either acetaldehyde or propanaldehyde.; mutation to L: Able to channel acetaldehyde but not the larger propanaldehyde.
P51016 4-hydroxy-2-oxovalerate aldolase; HOA; 4-hydroxy-2-keto-pentanoic acid aldolase; 4-hydroxy-2-oxopentanoate aldolase; EC 4.1.3.39 from Pseudomonas sp. (strain CF600) (see 2 papers)
51% identity, 96% coverage: 7:340/347 of query aligns to 3:336/345 of P51016
- D18 (= D22) binding Mn(2+)
- H200 (= H204) binding Mn(2+)
- H202 (= H206) binding Mn(2+)
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1nvmA Crystal structure of a bifunctional aldolase-dehydrogenase : sequestering a reactive and volatile intermediate (see paper)
51% identity, 96% coverage: 7:340/347 of query aligns to 2:335/340 of 1nvmA
- active site: D17 (= D22), H20 (= H25), H199 (= H204), H201 (= H206), Y290 (= Y295)
- binding manganese (ii) ion: D17 (= D22), H199 (= H204), H201 (= H206)
- binding oxalate ion: R16 (= R21), F138 (= F143), M140 (= M145), S170 (= S175), H199 (= H204), H201 (= H206), Y290 (= Y295)
3bliA Crystal structure of the catalytic domain of licms in complexed with pyruvate and acetyl-coa (see paper)
34% identity, 34% coverage: 152:268/347 of query aligns to 150:266/311 of 3bliA
Sites not aligning to the query:
Q8F3Q1 (R)-citramalate synthase CimA; LiCMS; EC 2.3.3.21 from Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) (see 2 papers)
34% identity, 34% coverage: 152:268/347 of query aligns to 156:272/516 of Q8F3Q1
- T179 (≠ S175) binding pyruvate; mutation to A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat.
Sites not aligning to the query:
- 16 mutation R->K,Q: Loss of activity.
- 16:17 binding pyruvate
- 17 D→A: 34-fold increase in Km for pyruvate and 315-fold decrease in kcat.; D→N: 4.4-fold increase in Km for pyruvate and 480-fold decrease in kcat.
- 81 L→A: 4.7-fold increase in Km for pyruvate and 15.7-fold decrease in kcat.; L→V: 3.3-fold increase in Km for pyruvate and 10.1-fold decrease in kcat.
- 83 F→A: 5-fold increase in Km for acetyl-CoA and 120-fold decrease in kcat.
- 104 L→V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
- 144 binding pyruvate; Y→L: 259-fold increase in Km for pyruvate and 76-fold decrease in kcat.; Y→V: 114-fold increase in Km for pyruvate and 5.3-fold decrease in kcat.
- 146 mutation E->D,Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat.
- 302 mutation H->A,N: Loss of activity.
- 304 D→A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
- 310 N→A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
- 311 L→A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
- 312 Y→A: Loss of activity.
- 430 Y→L: No change in Km for acetyl-CoA and 2.3-fold decrease in kcat. Severely impairs inhibition by isoleucine.
- 431 D→A: 1.8-fold decrease in Km for acetyl-CoA and 5-fold decrease in kcat.
- 451 L→V: 1.5-fold increase in Km for acetyl-CoA and 4.3 decrease in kcat.
- 454 Y→A: 1.4 decrease in Km for acetyl-CoA and 17-fold decrease in kcat. Still inhibited by isoleucine and weakly inhibited by leucine.
- 458 I→A: 1.3-fold decrease in Km for acetyl-CoA and 14-fold decrease in kcat. Abolishes inhibition by isoleucine.
- 464 T→A: 1.8-fold decrease in Km for acetyl-CoA and 4.3-fold decrease in kcat.
- 468 V→A: No change in Km for acetyl-CoA and 2-fold decrease in kcat. Increases inhibition by isoleucine and leucine becomes an effective inhibitor.
- 493 P→A: 1.5-fold decrease in Km for acetyl-CoA and 2.6-fold decrease in kcat.
- 495 Q→A: 1.6-fold decrease in Km for acetyl-CoA and 2.8-fold decrease in kcat.
Q9JZG1 2-isopropylmalate synthase; Alpha-IPM synthase; Alpha-isopropylmalate synthase; EC 2.3.3.13 from Neisseria meningitidis serogroup B (strain MC58) (see 2 papers)
30% identity, 52% coverage: 164:345/347 of query aligns to 162:355/517 of Q9JZG1
- H204 (= H204) binding Mn(2+)
- H206 (= H206) binding Mn(2+)
- N240 (= N240) binding Mn(2+)
Sites not aligning to the query:
- 16 binding Mn(2+)
- 366:517 Required for the condensation reaction. Not required to bind substrate
3rmjB Crystal structure of truncated alpha-isopropylmalate synthase from neisseria meningitidis (see paper)
30% identity, 36% coverage: 164:287/347 of query aligns to 159:292/308 of 3rmjB
Sites not aligning to the query:
5ks8C Crystal structure of two-subunit pyruvate carboxylase from methylobacillus flagellatus (see paper)
24% identity, 72% coverage: 13:261/347 of query aligns to 2:258/603 of 5ks8C
- active site: D11 (= D22), D115 (vs. gap), K172 (≠ V173), H201 (= H204), H203 (= H206)
- binding manganese (ii) ion: D11 (= D22), K172 (≠ V173), H201 (= H204), H203 (= H206)
- binding pyruvic acid: L79 (= L92), R81 (≠ L94), F114 (vs. gap), M174 (≠ S175)
5ks8D Crystal structure of two-subunit pyruvate carboxylase from methylobacillus flagellatus (see paper)
24% identity, 72% coverage: 13:261/347 of query aligns to 3:259/580 of 5ks8D
- active site: D12 (= D22), D116 (vs. gap), K173 (≠ V173), H202 (= H204), H204 (= H206)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: D51 (≠ N65), Y56 (≠ F68)
- binding manganese (ii) ion: D12 (= D22), K173 (≠ V173), H202 (= H204), H204 (= H206)
- binding pyruvic acid: Q15 (≠ H25), G47 (= G61), L80 (= L92), R82 (vs. gap)
Sites not aligning to the query:
1rqhA Propionibacterium shermanii transcarboxylase 5s subunit bound to pyruvic acid (see paper)
21% identity, 72% coverage: 12:261/347 of query aligns to 10:269/471 of 1rqhA
- active site: D20 (= D22), D124 (≠ T118), K181 (≠ V173), H212 (= H204), H214 (= H206)
- binding cobalt (ii) ion: D20 (= D22), K181 (≠ V173), H212 (= H204), H214 (= H206)
- binding pyruvic acid: Q23 (≠ K27), G55 (= G61), L88 (= L92), K181 (≠ V173)
Sites not aligning to the query:
1rr2A Propionibacterium shermanii transcarboxylase 5s subunit bound to 2- ketobutyric acid (see paper)
21% identity, 72% coverage: 12:261/347 of query aligns to 11:270/472 of 1rr2A
- active site: D21 (= D22), D125 (≠ T118), K182 (≠ V173), H213 (= H204), H215 (= H206)
- binding 2-ketobutyric acid: Q24 (≠ K27), G56 (= G61), L89 (= L92), K182 (≠ V173)
- binding cobalt (ii) ion: D21 (= D22), K182 (≠ V173), H213 (= H204), H215 (= H206)
Sites not aligning to the query:
1rqeA Propionibacterium shermanii transcarboxylase 5s subunit bound to oxaloacetate (see paper)
21% identity, 72% coverage: 12:261/347 of query aligns to 11:270/472 of 1rqeA