SitesBLAST
Comparing WP_011781545.1 NCBI__GCF_000015305.1:WP_011781545.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
8ih7A Amng-amnh complex
64% identity, 99% coverage: 3:335/337 of query aligns to 8:340/340 of 8ih7A
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)
65% identity, 99% coverage: 2:334/337 of query aligns to 6:338/345 of P51016
- D18 (= D14) binding Mn(2+)
- H200 (= H196) binding Mn(2+)
- H202 (= H198) 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)
65% identity, 99% coverage: 2:334/337 of query aligns to 5:337/340 of 1nvmA
- active site: D17 (= D14), H20 (= H17), H199 (= H196), H201 (= H198), Y290 (= Y287)
- binding manganese (ii) ion: D17 (= D14), H199 (= H196), H201 (= H198)
- binding oxalate ion: R16 (= R13), F138 (= F135), M140 (= M137), S170 (= S167), H199 (= H196), H201 (= H198), Y290 (= Y287)
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)
55% identity, 98% coverage: 5:333/337 of query aligns to 8:336/346 of P51015
- R16 (= R13) mutation to A: Loss of aldol cleavage activity.; mutation to K: 4000-fold decrease in the catalytic efficiency of the aldol cleavage reaction.
- H20 (= H17) 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 (= L84) 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 (= L86) 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 (= Y287) 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 (= G319) 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 (= G320) 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.
4jn6C Crystal structure of the aldolase-dehydrogenase complex from mycobacterium tuberculosis hrv37 (see paper)
50% identity, 98% coverage: 5:333/337 of query aligns to 4:332/339 of 4jn6C
- active site: D13 (= D14), H16 (= H17), H195 (= H196), H197 (= H198), Y286 (= Y287)
- binding manganese (ii) ion: D13 (= D14), H195 (= H196), H197 (= H198)
- binding oxalate ion: R12 (= R13), M136 (= M137), V164 (≠ T165), S166 (= S167), H195 (= H196), H197 (= H198), Y286 (= Y287)
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)
50% identity, 98% coverage: 5:333/337 of query aligns to 7:335/346 of P9WMK5
- D16 (= D14) binding Mn(2+)
- H198 (= H196) binding Mn(2+)
- H200 (= H198) binding Mn(2+)
- G322 (= G320) mutation to F: Abolishes substrate channeling to HsaG.
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)
50% identity, 97% coverage: 7:333/337 of query aligns to 13:338/347 of Q53WI0
- A324 (≠ G319) mutation to G: Increases the channeling efficiency of propanaldehyde from 57% to 94%.
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
48% identity, 98% coverage: 5:333/337 of query aligns to 4:332/337 of 4lrsA
- active site: D13 (= D14), H16 (= H17), H195 (= H196), H197 (= H198), Y286 (= Y287)
- binding magnesium ion: D13 (= D14), H195 (= H196), H197 (= H198)
- binding pyruvic acid: R12 (= R13), D13 (= D14), F134 (= F135), M136 (= M137), V164 (≠ T165), S166 (= S167), H195 (= H196), H197 (= H198), Y286 (= Y287)
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)
27% identity, 82% coverage: 1:276/337 of query aligns to 3:287/517 of Q9JZG1
- D16 (= D14) binding Mn(2+)
- H204 (= H196) binding Mn(2+)
- H206 (= H198) binding Mn(2+)
- N240 (= N232) binding Mn(2+)
Sites not aligning to the query:
- 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)
27% identity, 82% coverage: 2:276/337 of query aligns to 1:284/308 of 3rmjB
Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
27% identity, 70% coverage: 5:239/337 of query aligns to 85:335/506 of Q9FG67
- S102 (≠ R22) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
- A290 (≠ G194) mutation to T: In gsm1-2; loss of conversion of C3 to C4 glucosinolates.
Q9FN52 Methylthioalkylmalate synthase 3, chloroplastic; 2-isopropylmalate synthase 2; Methylthioalkylmalate synthase-like; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
26% identity, 70% coverage: 5:239/337 of query aligns to 85:335/503 of Q9FN52
- G263 (= G169) mutation to E: In gsm2-1; loss of activity and lack of C6, C7 and C8 aliphatic glucosinolates.
6ktqA Crystal structure of catalytic domain of homocitrate synthase from sulfolobus acidocaldarius (sahcs(dram)) in complex with alpha- ketoglutarate/zn2+/coa (see paper)
29% identity, 45% coverage: 109:261/337 of query aligns to 126:278/399 of 6ktqA
Sites not aligning to the query:
5ks8D Crystal structure of two-subunit pyruvate carboxylase from methylobacillus flagellatus (see paper)
26% identity, 75% coverage: 5:258/337 of query aligns to 3:264/580 of 5ks8D
- active site: D12 (= D14), D116 (≠ T110), K173 (≠ T165), H202 (= H196), H204 (= H198)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: D51 (≠ G53), Y56 (= Y58)
- binding manganese (ii) ion: D12 (= D14), K173 (≠ T165), H202 (= H196), H204 (= H198)
- binding pyruvic acid: Q15 (≠ H17), G47 (≠ D49), L80 (= L85), R82 (≠ P87)
Sites not aligning to the query:
5ks8C Crystal structure of two-subunit pyruvate carboxylase from methylobacillus flagellatus (see paper)
26% identity, 75% coverage: 5:258/337 of query aligns to 2:263/603 of 5ks8C
- active site: D11 (= D14), D115 (≠ T110), K172 (≠ T165), H201 (= H196), H203 (= H198)
- binding manganese (ii) ion: D11 (= D14), K172 (≠ T165), H201 (= H196), H203 (= H198)
- binding pyruvic acid: L79 (= L85), R81 (≠ P87), F114 (≠ A109), M174 (≠ S167)
2nx9B Crystal structure of the carboxyltransferase domain of the oxaloacetate decarboxylase na+ pump from vibrio cholerae (see paper)
24% identity, 76% coverage: 5:260/337 of query aligns to 7:270/453 of 2nx9B
Sites not aligning to the query:
P35914 Hydroxymethylglutaryl-CoA lyase, mitochondrial; HL; HMG-CoA lyase; 3-hydroxy-3-methylglutarate-CoA lyase; EC 4.1.3.4 from Homo sapiens (Human) (see 11 papers)
28% identity, 41% coverage: 144:281/337 of query aligns to 182:325/325 of P35914
- F192 (≠ M154) to S: in HMGCLD; activity lower than 5% respect to the wild-type
- I200 (≠ V162) to F: in HMGCLD; activity lower than 5% respect to the wild-type
- G203 (≠ T165) to E: in HMGCLD; complete loss of activity; dbSNP:rs1553131940
- D204 (= D166) mutation to A: Reduced activity, and reduced affinity for metal cofactor and substrate.
- H233 (= H196) to R: in HMGCLD; loss of activity; dbSNP:rs727503963; mutation to A: Loss of activity, and reduced proton exchange rate.
- E279 (= E236) mutation to A: Reduced thermal stability, but normal activity.
- D280 (≠ P237) mutation to A: Normal activity.
- C323 (≠ L279) modified: Interchain; mutation to S: Abolishes interchain homodimerization. Exhibits no DTT stimulated activity.
Sites not aligning to the query:
- 37 E → K: in HMGCLD; activity lower than 5% respect to the wild-type; E→D: Normal activity.
- 41 R → Q: in HMGCLD; loss of activity and of proton exchange; dbSNP:rs121964997; R→M: Reduced activity, and loss of proton exchange.
- 42 D → E: in HMGCLD; reduced activity; D → G: in HMGCLD; loss of activity; dbSNP:rs1467902610; D → H: in HMGCLD; loss of activity; mutation D->A,N: Loss of activity, and reduced proton exchange rate.
- 48 K → N: in HMGCLD; abolishes almost all enzymatic activity
- 72 E→A: Loss of activity, and reduced affinity for metal cofactor and substrate.
- 142 S → F: in HMGCLD; activity lower than 5% respect to the wild-type
- 174 C → Y: in HMGCLD; activity lower than 5% respect to the wild-type; dbSNP:rs765475941
1rqhA Propionibacterium shermanii transcarboxylase 5s subunit bound to pyruvic acid (see paper)
24% identity, 36% coverage: 157:279/337 of query aligns to 173:294/471 of 1rqhA
Sites not aligning to the query:
Q70AC7 Methylmalonyl-CoA carboxyltransferase 5S subunit; Transcarboxylase 5S subunit; EC 2.1.3.1 from Propionibacterium freudenreichii subsp. shermanii (see paper)
24% identity, 36% coverage: 157:279/337 of query aligns to 176:297/505 of Q70AC7
- K184 (≠ T165) modified: N6-carboxylysine; partial; mutation K->A,E: Loss of activity.
- M186 (≠ S167) mutation to I: Decreases activity by 98%.
Sites not aligning to the query:
- 59 A→T: Decreases activity by 96%.
1rr2A Propionibacterium shermanii transcarboxylase 5s subunit bound to 2- ketobutyric acid (see paper)
24% identity, 36% coverage: 157:279/337 of query aligns to 174:295/472 of 1rr2A
Sites not aligning to the query:
Query Sequence
>WP_011781545.1 NCBI__GCF_000015305.1:WP_011781545.1
MTTTVYVQDVTLRDGMHAIRHRISPRNVARIAAALDRAGVDAIEVAHGDGLAGSSLSYGP
GSHTDWEWIDAVAGAVTNATVTTLLLPGIGTVAQLDEAYRRGVRSVRVATHCTEADIAAQ
HIAHARELGMDVSGFLMMSHMAQPADLAAQAKLMESFGAQSVYVTDSGGRLTMHDVRDRV
LAYRDVLAPSTQIGIHAHENLSLAVANSVAAVEAGATRVDASLAGQGAGAGNCPIEPFVA
VADLFGWKHGCDLFALQDAADDIVRPLRDRPVRVDRETLTLGFAGVYSSFLRHAEDASAR
YGVDTRAILVEVGRRGLIGGQEDMIVDIALSLSAGVP
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