SitesBLAST
Comparing AO353_15115 FitnessBrowser__pseudo3_N2E3:AO353_15115 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)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
29% identity, 96% coverage: 8:449/462 of query aligns to 7:473/485 of 2f2aA
- active site: K79 (= K80), S154 (= S155), S155 (= S156), S173 (≠ T174), T175 (≠ I176), G176 (= G177), G177 (= G178), S178 (= S179), Q181 (≠ L182)
- binding glutamine: G130 (≠ L131), S154 (= S155), D174 (= D175), T175 (≠ I176), G176 (= G177), S178 (= S179), F206 (≠ P203), Y309 (vs. gap), Y310 (vs. gap), R358 (= R334), D425 (≠ I400)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
29% identity, 96% coverage: 8:449/462 of query aligns to 7:473/485 of 2dqnA
- active site: K79 (= K80), S154 (= S155), S155 (= S156), S173 (≠ T174), T175 (≠ I176), G176 (= G177), G177 (= G178), S178 (= S179), Q181 (≠ L182)
- binding asparagine: M129 (= M130), G130 (≠ L131), T175 (≠ I176), G176 (= G177), S178 (= S179), Y309 (vs. gap), Y310 (vs. gap), R358 (= R334), D425 (≠ I400)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
28% identity, 94% coverage: 16:449/462 of query aligns to 138:588/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (= G129), T258 (≠ S132), S281 (= S155), G302 (≠ I176), G303 (= G177), S305 (= S179), S472 (≠ Q325), I532 (≠ P393), M539 (≠ I400)
Sites not aligning to the query:
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
28% identity, 94% coverage: 16:449/462 of query aligns to 138:588/607 of Q7XJJ7
- K205 (= K80) mutation to A: Loss of activity.
- SS 281:282 (= SS 155:156) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ IGGS 176:179) binding
- S305 (= S179) mutation to A: Loss of activity.
- R307 (= R181) mutation to A: Loss of activity.
- S360 (≠ P230) mutation to A: No effect.
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
30% identity, 97% coverage: 2:449/462 of query aligns to 1:473/490 of 4yjiA
- active site: K79 (= K80), S158 (= S155), S159 (= S156), G179 (≠ I176), G180 (= G177), G181 (= G178), A182 (≠ S179)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L82), G132 (= G129), S158 (= S155), G179 (≠ I176), G180 (= G177), A182 (≠ S179)
3kfuE Crystal structure of the transamidosome (see paper)
33% identity, 97% coverage: 9:457/462 of query aligns to 2:462/468 of 3kfuE
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 92% coverage: 26:450/462 of query aligns to 28:467/478 of 3h0mA
- active site: K72 (= K80), S147 (= S155), S148 (= S156), S166 (≠ T174), T168 (≠ I176), G169 (= G177), G170 (= G178), S171 (= S179), Q174 (≠ L182)
- binding glutamine: M122 (= M130), G123 (≠ L131), D167 (= D175), T168 (≠ I176), G169 (= G177), G170 (= G178), S171 (= S179), F199 (≠ P203), Y302 (vs. gap), R351 (≠ W336), D418 (≠ I400)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 92% coverage: 26:450/462 of query aligns to 28:467/478 of 3h0lA
- active site: K72 (= K80), S147 (= S155), S148 (= S156), S166 (≠ T174), T168 (≠ I176), G169 (= G177), G170 (= G178), S171 (= S179), Q174 (≠ L182)
- binding asparagine: G123 (≠ L131), S147 (= S155), G169 (= G177), G170 (= G178), S171 (= S179), Y302 (vs. gap), R351 (≠ W336), D418 (≠ I400)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
26% identity, 96% coverage: 7:449/462 of query aligns to 5:444/457 of 5h6sC
- active site: K77 (= K80), S152 (= S155), S153 (= S156), L173 (≠ I176), G174 (= G177), G175 (= G178), S176 (= S179)
- binding 4-oxidanylbenzohydrazide: C126 (≠ G129), R128 (≠ L131), W129 (≠ S132), S152 (= S155), L173 (≠ I176), G174 (= G177), S176 (= S179), W306 (= W315), F338 (vs. gap)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
29% identity, 85% coverage: 69:462/462 of query aligns to 84:507/508 of 3a1iA
- active site: K95 (= K80), S170 (= S155), S171 (= S156), G189 (≠ T174), Q191 (≠ I176), G192 (= G177), G193 (= G178), A194 (≠ S179), I197 (≠ L182)
- binding benzamide: F145 (≠ M130), S146 (≠ L131), G147 (≠ S132), Q191 (≠ I176), G192 (= G177), G193 (= G178), A194 (≠ S179), W327 (vs. gap)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
28% identity, 95% coverage: 10:450/462 of query aligns to 9:477/487 of 1m21A
- active site: K81 (= K80), S160 (= S155), S161 (= S156), T179 (= T174), T181 (≠ I176), D182 (≠ G177), G183 (= G178), S184 (= S179), C187 (≠ L182)
- binding : A129 (≠ G129), N130 (≠ M130), F131 (≠ L131), C158 (≠ G153), G159 (= G154), S160 (= S155), S184 (= S179), C187 (≠ L182), I212 (vs. gap), R318 (= R300), L321 (= L303), L365 (≠ A337), F426 (≠ Q395)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
27% identity, 94% coverage: 18:449/462 of query aligns to 16:468/482 of 3a2qA
- active site: K69 (= K80), S147 (= S155), S148 (= S156), N166 (≠ T174), A168 (≠ I176), A169 (≠ G177), G170 (= G178), A171 (≠ S179), I174 (≠ L182)
- binding 6-aminohexanoic acid: G121 (= G129), G121 (= G129), N122 (≠ M130), S147 (= S155), A168 (≠ I176), A168 (≠ I176), A169 (≠ G177), A171 (≠ S179), C313 (≠ W310)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
27% identity, 97% coverage: 6:453/462 of query aligns to 29:491/507 of Q84DC4
- T31 (= T8) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K80) mutation to A: Abolishes activity on mandelamide.
- S180 (= S155) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S156) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G177) 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 (= S179) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ L182) 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 (≠ A301) 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 (≠ F352) 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 (≠ V404) 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.
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
32% identity, 55% coverage: 7:260/462 of query aligns to 1:260/457 of 6c6gA
Q9TUI8 Fatty-acid amide hydrolase 1; Anandamide amidase; Anandamide amidohydrolase 1; Fatty acid ester hydrolase; Oleamide hydrolase 1; EC 3.5.1.99; EC 3.1.1.- from Sus scrofa (Pig) (see paper)
37% identity, 49% coverage: 69:296/462 of query aligns to 131:365/579 of Q9TUI8
- S217 (= S155) mutation to A: Loss of activity.
- S218 (= S156) mutation to A: Lowers activity by at least 98%.
- D237 (= D175) mutation D->E,N: Loss of activity.
- S241 (= S179) mutation to A: Loss of activity.
- C249 (= C187) mutation to A: Loss of activity.
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)
28% identity, 52% coverage: 72:309/462 of query aligns to 28:269/425 of Q9FR37
- K36 (= K80) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S155) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S156) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D175) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S179) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C187) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (≠ G254) mutation to T: Slightly reduces catalytic activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
29% identity, 86% coverage: 50:445/462 of query aligns to 45:434/461 of 4gysB
- active site: K72 (= K80), S146 (= S155), S147 (= S156), T165 (= T174), T167 (≠ I176), A168 (≠ G177), G169 (= G178), S170 (= S179), V173 (≠ L182)
- binding malonate ion: A120 (≠ G129), G122 (≠ L131), S146 (= S155), T167 (≠ I176), A168 (≠ G177), S170 (= S179), S193 (≠ A210), G194 (= G211), V195 (vs. gap), R200 (= R215), Y297 (≠ L306), R305 (≠ Q314)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
27% identity, 94% coverage: 7:438/462 of query aligns to 2:395/412 of 1o9oA
- active site: K62 (= K80), A131 (≠ S155), S132 (= S156), T150 (= T174), T152 (≠ I176), G153 (= G177), G154 (= G178), S155 (= S179), R158 (≠ L182)
- binding 3-amino-3-oxopropanoic acid: G130 (= G154), T152 (≠ I176), G153 (= G177), G154 (= G178), S155 (= S179), R158 (≠ L182), P359 (= P393)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
27% identity, 94% coverage: 7:438/462 of query aligns to 2:395/412 of 1ocmA
- active site: K62 (= K80), S131 (= S155), S132 (= S156), T152 (≠ I176), G153 (= G177), G154 (= G178), S155 (= S179)
- binding pyrophosphate 2-: R113 (≠ S137), S131 (= S155), Q151 (≠ D175), T152 (≠ I176), G153 (= G177), G154 (= G178), S155 (= S179), R158 (≠ L182), P359 (= P393)
3qkvA Crystal structure of fatty acid amide hydrolase with small molecule compound (see paper)
40% identity, 32% coverage: 69:218/462 of query aligns to 103:260/549 of 3qkvA
- active site: K114 (= K80), S189 (= S155), S190 (= S156), T208 (= T174), I210 (= I176), G211 (= G177), G212 (= G178), S213 (= S179), F216 (≠ L182)
- binding (6-bromo-1'H,4H-spiro[1,3-benzodioxine-2,4'-piperidin]-1'-yl)methanol: L164 (= L131), S165 (= S132), I210 (= I176), G211 (= G177), S213 (= S179)
Sites not aligning to the query:
Query Sequence
>AO353_15115 FitnessBrowser__pseudo3_N2E3:AO353_15115
MSDLHTLTAAELLARFASRQLTPIDYYDQLLTHIDRWEPQINALYAFDPQQVRQQAQAST
ERWNKGQPNGALDGVPVTLKELIATEGQPIPLGSAATRLTPALKDAPPAARLREAGAIIL
AKTTVPDFGMLSSGLSSFHGITRNPWNTANNPGGSSAGAAAAAAAGYGPLHVGTDIGGSV
RLPAAWCGLVGFKPTLGRIPIDPYYTGRTAGPMTRTVDDCVLLMQHLARPDSRDATSLPP
LTTPWSNQPLSVKGLRVGLMLEPGAGLAPEAFVCNAVEQAARLFEAHGAKVTVIAPIMDR
AQLDGLDQFWRARQWAELSALSSEQFDRVLPYIRDWAAPGADITGVEAVRGFNQTFEMRR
RAAQLFDTFDLVLSPTNQINAFAADWPSPSNDPQQPFEHIVFTVPWNMGEQPALSINCGF
AADGMPIGLQMIAPRFADQWLLQIAKTYENWRGAIHCWPSPA
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