SitesBLAST
Comparing WP_010441557.1 NCBI__GCF_000192475.1:WP_010441557.1 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)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
36% identity, 97% coverage: 11:425/429 of query aligns to 6:410/412 of 1o9oA
- active site: K62 (= K76), A131 (≠ S145), S132 (= S146), T150 (≠ S164), T152 (= T166), G153 (≠ A167), G154 (≠ A168), S155 (= S169), R158 (= R172)
- binding 3-amino-3-oxopropanoic acid: G130 (= G144), T152 (= T166), G153 (≠ A167), G154 (≠ A168), S155 (= S169), R158 (= R172), P359 (= P373)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
37% identity, 97% coverage: 11:425/429 of query aligns to 6:410/412 of 1ocmA
- active site: K62 (= K76), S131 (= S145), S132 (= S146), T152 (= T166), G153 (≠ A167), G154 (≠ A168), S155 (= S169)
- binding pyrophosphate 2-: R113 (≠ F127), S131 (= S145), Q151 (= Q165), T152 (= T166), G153 (≠ A167), G154 (≠ A168), S155 (= S169), R158 (= R172), P359 (= P373)
3kfuE Crystal structure of the transamidosome (see paper)
33% identity, 96% coverage: 9:418/429 of query aligns to 2:450/468 of 3kfuE
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
28% identity, 95% coverage: 7:415/429 of query aligns to 6:465/485 of 2f2aA
- active site: K79 (= K76), S154 (= S145), S155 (= S146), S173 (= S164), T175 (= T166), G176 (≠ A167), G177 (≠ A168), S178 (= S169), Q181 (≠ R172)
- binding glutamine: G130 (vs. gap), S154 (= S145), D174 (≠ Q165), T175 (= T166), G176 (≠ A167), S178 (= S169), F206 (≠ L197), Y309 (≠ H288), Y310 (≠ H289), R358 (vs. gap), D425 (vs. gap)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
28% identity, 95% coverage: 7:415/429 of query aligns to 6:465/485 of 2dqnA
- active site: K79 (= K76), S154 (= S145), S155 (= S146), S173 (= S164), T175 (= T166), G176 (≠ A167), G177 (≠ A168), S178 (= S169), Q181 (≠ R172)
- binding asparagine: M129 (vs. gap), G130 (vs. gap), T175 (= T166), G176 (≠ A167), S178 (= S169), Y309 (≠ H288), Y310 (≠ H289), R358 (vs. gap), D425 (vs. gap)
Q9FR37 Amidase 1; AtAMI1; Translocon at the outer membrane of chloroplasts 64-I; AtTOC64-I; EC 3.5.1.4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
29% identity, 82% coverage: 68:417/429 of query aligns to 28:417/425 of Q9FR37
- K36 (= K76) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S145) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S146) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (≠ Q165) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S169) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C177) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (= S240) mutation to T: Slightly reduces catalytic activity.
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
31% identity, 96% coverage: 15:425/429 of query aligns to 36:490/507 of Q84DC4
- K100 (= K76) mutation to A: Abolishes activity on mandelamide.
- S180 (= S145) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S146) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ A167) mutation to A: Increase in KM values for aromatic substrates, but not aliphatic substrates. Active against lactamide but not against mandelamide; when associated with H-207 and E-382.; mutation to V: Increase in KM values for aromatic substrates, but not aliphatic substrates.
- S204 (= S169) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ R172) mutation to H: Increases activity on lactamide, does not affect activity on mandelamide; when associated with E-382. Active against lactamide but not against mandelamide; when associated with A-202 and E-382. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with S-316 and N-437.
- S316 (≠ A276) mutation to N: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with H-207 and N-437.
- Q382 (vs. gap) mutation to H: Increases activity on lactamide, does not affect activity on mandelamide; when associated with H-207. Active against lactamide but not against mandelamide; when associated with A-202 and H-207.
- I437 (≠ W379) mutation to N: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with I-31. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with H-207 and N-316.
Sites not aligning to the query:
- 31 T→I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
27% identity, 97% coverage: 10:424/429 of query aligns to 132:590/607 of Q7XJJ7
- K205 (= K76) mutation to A: Loss of activity.
- SS 281:282 (= SS 145:146) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TAAS 166:169) binding substrate
- S305 (= S169) mutation to A: Loss of activity.
- R307 (≠ I171) mutation to A: Loss of activity.
- S360 (≠ I224) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
27% identity, 97% coverage: 10:424/429 of query aligns to 132:590/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A125), T258 (≠ R128), S281 (= S145), G302 (≠ T166), G303 (≠ A167), S305 (= S169), S472 (≠ L318), I532 (≠ L367), M539 (≠ L374)
Sites not aligning to the query:
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
26% identity, 97% coverage: 10:424/429 of query aligns to 132:590/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A125), G302 (≠ T166), G303 (≠ A167), G304 (≠ A168), A305 (≠ S169), V442 (≠ H289), I475 (≠ A321), M539 (≠ L374)
Sites not aligning to the query:
8ey1D Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with n-(3-oxododecanoyl)-l-homoserine lactone
26% identity, 97% coverage: 10:424/429 of query aligns to 132:590/605 of 8ey1D
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
25% identity, 97% coverage: 4:418/429 of query aligns to 2:462/478 of 3h0mA
- active site: K72 (= K76), S147 (= S145), S148 (= S146), S166 (= S164), T168 (= T166), G169 (≠ A167), G170 (≠ A168), S171 (= S169), Q174 (≠ R172)
- binding glutamine: M122 (vs. gap), G123 (vs. gap), D167 (≠ Q165), T168 (= T166), G169 (≠ A167), G170 (≠ A168), S171 (= S169), F199 (≠ L197), Y302 (vs. gap), R351 (≠ L318), D418 (≠ N380)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
25% identity, 97% coverage: 4:418/429 of query aligns to 2:462/478 of 3h0lA
- active site: K72 (= K76), S147 (= S145), S148 (= S146), S166 (= S164), T168 (= T166), G169 (≠ A167), G170 (≠ A168), S171 (= S169), Q174 (≠ R172)
- binding asparagine: G123 (vs. gap), S147 (= S145), G169 (≠ A167), G170 (≠ A168), S171 (= S169), Y302 (vs. gap), R351 (≠ L318), D418 (≠ N380)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
37% identity, 50% coverage: 11:224/429 of query aligns to 10:236/487 of 1m21A
- active site: K81 (= K76), S160 (= S145), S161 (= S146), T179 (≠ S164), T181 (= T166), D182 (≠ A167), G183 (≠ A168), S184 (= S169), C187 (≠ R172)
- binding : A129 (= A125), N130 (≠ Y126), F131 (= F127), C158 (≠ G143), G159 (= G144), S160 (= S145), S184 (= S169), C187 (≠ R172), I212 (≠ L197)
Sites not aligning to the query:
Q9AHE8 Urethanase; Enantioselective amidase; Ethyl carbamate-degrading amidase; EC 3.5.1.75 from Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium radiobacter) (see 3 papers)
25% identity, 82% coverage: 64:415/429 of query aligns to 86:502/517 of Q9AHE8
- R94 (≠ P72) mutation to P: No change in activity.
- I97 (= I75) mutation to L: 1.12-fold increase in specific activity toward ethyl carbamate, shows higher ethanol tolerance. 3.1-fold increase in specific activity toward ethyl carbamate and 1.5-fold increase in ethanol tolerance, shows lower pH tolerance; when associated with A-195.
- K98 (= K76) mutation to A: Almost loss of activity.
- P163 (= P135) mutation to A: Decrease in activity.
- A172 (≠ G144) mutation to G: Changes substrate specificity. Decrease in activity.
- S173 (= S145) mutation to A: Almost loss of activity.
- N175 (≠ S147) mutation to G: Decrease in activity.; mutation to S: Changes substrate specificity.
- G195 (≠ A167) mutation to A: 1.86-fold increase in specific activity toward ethyl carbamate, shows lower pH tolerance, causes a decrease in the thermostability. 3.1-fold increase in specific activity toward ethyl carbamate and 1.5-fold increase in ethanol tolerance, shows lower pH tolerance; when associated with L-97.
- S197 (= S169) mutation to A: Almost loss of activity.
- L200 (≠ R172) mutation to C: Decrease in activity.
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
29% identity, 89% coverage: 25:406/429 of query aligns to 19:432/457 of 6c6gA
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
31% identity, 81% coverage: 59:405/429 of query aligns to 71:444/605 of Q936X2
- K91 (= K76) mutation to A: Loss of activity.
- S165 (= S145) mutation to A: Loss of activity.
- S189 (= S169) mutation to A: Loss of activity.
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
28% identity, 87% coverage: 24:397/429 of query aligns to 22:428/457 of 5h6sC
- active site: K77 (= K76), S152 (= S145), S153 (= S146), L173 (≠ T166), G174 (≠ A167), G175 (≠ A168), S176 (= S169)
- binding 4-oxidanylbenzohydrazide: C126 (≠ T119), R128 (≠ T121), W129 (≠ T122), S152 (= S145), L173 (≠ T166), G174 (≠ A167), S176 (= S169), W306 (vs. gap), F338 (≠ A321)
Q9MUK5 Translocon at the outer membrane of chloroplasts 64 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
24% identity, 83% coverage: 73:426/429 of query aligns to 66:455/593 of Q9MUK5
Sites not aligning to the query:
- 516 N→A: Loss of HSP90 binding, but no effect on HSP70 binding.
- 550 R→A: 80% decrease of HSP70 and HSP90 binding.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
28% identity, 91% coverage: 37:427/429 of query aligns to 44:443/461 of 4gysB
- active site: K72 (= K76), S146 (= S145), S147 (= S146), T165 (≠ S164), T167 (= T166), A168 (= A167), G169 (≠ A168), S170 (= S169), V173 (≠ R172)
- binding malonate ion: A120 (= A125), G122 (≠ F127), S146 (= S145), T167 (= T166), A168 (= A167), S170 (= S169), S193 (≠ F192), G194 (= G193), V195 (= V194), R200 (≠ P199), Y297 (≠ M292), R305 (= R298)
Query Sequence
>WP_010441557.1 NCBI__GCF_000192475.1:WP_010441557.1
MSDLCRRSAHDLARLIRIREVKPSEVMQAHLERIALREPVLGAFQYLDADRAMDRALAAD
NRQSDGPLHGVPFVIKDIIDTDDMPTGWGSDLYSNRQPVMNAACVQMLLDVGAIPIGKTV
TTEFAYFRPGKTANPHNPEHTPGGSSSGSAAAVADFMAPLAFGSQTAASLIRPAAYCGVY
GFRPTIHGYPLFGVMGLSPSLDTLGVLARHPYDLALTDAVLRGIESPQRARFEDSLPRIS
LMRGPHWMDGSIEMRDTCTRAMSAIAAAGSDSGEIAHPAILADLTAAHHTIMAYEAARLR
LDEFEKGLPAISPQFHALIEAGLKISEADYQHALILRDRAELVLEQIFGDTDALLVPSAP
GSAPVGLEATGDPLFSRMWNLLQVPSIAIPFGVNQNGLPLGIQLVAPKGYDARLLDIAQW
VSNILNPLG
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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