SitesBLAST
Comparing AO353_29150 FitnessBrowser__pseudo3_N2E3:AO353_29150 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 17 hits to proteins with known functional sites (download)
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
88% identity, 99% coverage: 3:566/568 of query aligns to 1:564/564 of 6te4A
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
28% identity, 98% coverage: 6:560/568 of query aligns to 5:485/487 of 1m21A
- active site: K81 (= K84), S160 (= S162), S161 (= S163), T179 (≠ E181), T181 (= T183), D182 (≠ W184), G183 (≠ S185), S184 (= S186), C187 (≠ G189)
- binding : A129 (= A133), N130 (= N134), F131 (vs. gap), C158 (≠ S160), G159 (= G161), S160 (= S162), S184 (= S186), C187 (≠ G189), I212 (≠ L214), R318 (= R352), L321 (≠ A355), L365 (≠ P413), F426 (≠ I488)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
37% identity, 43% coverage: 16:260/568 of query aligns to 10:249/457 of 6c6gA
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
26% identity, 97% coverage: 12:560/568 of query aligns to 8:443/461 of 4gysB
- active site: K72 (= K84), S146 (= S162), S147 (= S163), T165 (≠ E181), T167 (= T183), A168 (≠ W184), G169 (≠ S185), S170 (= S186), V173 (≠ G189)
- binding malonate ion: A120 (= A133), G122 (= G135), S146 (= S162), T167 (= T183), A168 (≠ W184), S170 (= S186), S193 (≠ R209), G194 (= G210), V195 (≠ N211), R200 (≠ P216), Y297 (≠ P353), R305 (= R361)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
33% identity, 40% coverage: 3:231/568 of query aligns to 1:227/457 of 5h6sC
- active site: K77 (= K84), S152 (= S162), S153 (= S163), L173 (≠ T183), G174 (≠ W184), G175 (≠ S185), S176 (= S186)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A133), R128 (≠ N134), W129 (≠ G135), S152 (= S162), L173 (≠ T183), G174 (≠ W184), S176 (= S186)
Sites not aligning to the query:
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
32% identity, 41% coverage: 6:239/568 of query aligns to 27:256/507 of Q84DC4
- T31 (≠ A10) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K84) mutation to A: Abolishes activity on mandelamide.
- S180 (= S162) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S163) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ W184) 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 (= S186) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ G189) 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.
Sites not aligning to the query:
- 316 S→N: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with H-207 and N-437.
- 382 Q→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.
- 437 I→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.
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
24% identity, 58% coverage: 9:337/568 of query aligns to 7:348/478 of 3h0mA
- active site: K72 (= K84), S147 (≠ F158), S148 (≠ A159), S166 (≠ E181), T168 (= T183), G169 (≠ W184), G170 (≠ S185), S171 (= S186), Q174 (≠ G189)
- binding glutamine: M122 (≠ N134), G123 (= G135), D167 (≠ E182), T168 (= T183), G169 (≠ W184), G170 (≠ S185), S171 (= S186), F199 (≠ L214), Y302 (≠ M289)
Sites not aligning to the query:
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
24% identity, 58% coverage: 9:337/568 of query aligns to 7:348/478 of 3h0lA
- active site: K72 (= K84), S147 (≠ F158), S148 (≠ A159), S166 (≠ E181), T168 (= T183), G169 (≠ W184), G170 (≠ S185), S171 (= S186), Q174 (≠ G189)
- binding asparagine: G123 (= G135), S147 (≠ F158), G169 (≠ W184), G170 (≠ S185), S171 (= S186), Y302 (≠ M289)
Sites not aligning to the query:
3kfuE Crystal structure of the transamidosome (see paper)
27% identity, 41% coverage: 11:243/568 of query aligns to 4:221/468 of 3kfuE
Sites not aligning to the query:
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
23% identity, 53% coverage: 35:337/568 of query aligns to 28:355/485 of 2f2aA
- active site: K79 (= K84), S154 (= S160), S155 (≠ G161), S173 (≠ E181), T175 (= T183), G176 (≠ W184), G177 (≠ S185), S178 (= S186), Q181 (≠ G189)
- binding glutamine: G130 (= G135), S154 (= S160), D174 (≠ E182), T175 (= T183), G176 (≠ W184), S178 (= S186), F206 (≠ L214), Y309 (≠ M289), Y310 (= Y290)
Sites not aligning to the query:
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
23% identity, 53% coverage: 35:337/568 of query aligns to 28:355/485 of 2dqnA
- active site: K79 (= K84), S154 (= S160), S155 (≠ G161), S173 (≠ E181), T175 (= T183), G176 (≠ W184), G177 (≠ S185), S178 (= S186), Q181 (≠ G189)
- binding asparagine: M129 (≠ N134), G130 (= G135), T175 (= T183), G176 (≠ W184), S178 (= S186), Y309 (≠ M289), Y310 (= Y290)
Sites not aligning to the query:
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
34% identity, 29% coverage: 66:229/568 of query aligns to 74:242/605 of Q936X2
- K91 (= K84) mutation to A: Loss of activity.
- S165 (≠ F158) mutation to A: Loss of activity.
- S189 (= S186) mutation to A: Loss of activity.
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
25% identity, 43% coverage: 15:257/568 of query aligns to 137:376/607 of Q7XJJ7
- K205 (= K84) mutation to A: Loss of activity.
- SS 281:282 (= SS 162:163) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TWSS 183:186) binding
- S305 (= S186) mutation to A: Loss of activity.
- R307 (= R188) mutation to A: Loss of activity.
- S360 (≠ E241) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
25% identity, 43% coverage: 15:257/568 of query aligns to 137:376/616 of 6diiH
Sites not aligning to the query:
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
32% identity, 40% coverage: 16:243/568 of query aligns to 14:231/482 of 3a2qA
- active site: K69 (= K84), S147 (= S162), S148 (= S163), N166 (≠ E181), A168 (≠ T183), A169 (≠ W184), G170 (≠ S185), A171 (≠ S186), I174 (≠ G189)
- binding 6-aminohexanoic acid: G121 (≠ A133), G121 (≠ A133), N122 (= N134), S147 (= S162), A168 (≠ T183), A168 (≠ T183), A169 (≠ W184), A171 (≠ S186)
Sites not aligning to the query:
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)
33% identity, 29% coverage: 76:242/568 of query aligns to 28:193/425 of Q9FR37
- K36 (= K84) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S162) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S163) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (≠ E182) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S186) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (≠ N194) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 214 S→T: Slightly reduces catalytic activity.
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
28% identity, 30% coverage: 74:242/568 of query aligns to 85:250/508 of 3a1iA
- active site: K95 (= K84), S170 (= S162), S171 (= S163), G189 (≠ E181), Q191 (≠ T183), G192 (≠ W184), G193 (≠ S185), A194 (≠ S186), I197 (≠ G189)
- binding benzamide: F145 (≠ N134), S146 (≠ G135), G147 (= G136), Q191 (≠ T183), G192 (≠ W184), G193 (≠ S185), A194 (≠ S186)
Sites not aligning to the query:
Query Sequence
>AO353_29150 FitnessBrowser__pseudo3_N2E3:AO353_29150
MIEVTEVPIAQLRAALESGQTTAVELVQAYLARIDAYDGPDTPTALNAVVVRNPEALNEA
RASDARRAKGQTLGPLDGIPYTAKDSYLVKGLTAASGSPAFANLIAYRDAFTIERLRAAG
AICLGKTNMPPMANGGMQRGVYGRAESPYNADYLTAPFASGSSNGAGTATAASFAAFGLA
EETWSSGRGPASNNGLCAYTPSRGVISVRGNWPLTPTMDVVVPFARTMADLLEVLDVVVA
EDPDTRGDLWRMQPWVPIPSVTSVRPASYVALAANPDALAGKRFGIPRMYINADPEAGTS
EAPGIGGPTGQRINTRASVIGLWEQARQALEAAGAEVIDVDFPLVSNCEGDRPGAPTVFN
RGIVSKEFLHDELWDLTAWAFDDFLQANGDPKLNRLVDVNGPLIFPHDPGTLPNREGDLA
AGMDEYVRMAERGITPWDQISTVPDGLRGLEQTRKIDLEDWMDKLGLDAVLFPTVADVGP
ANADVDPISADIAWSNGIWVANGNLAIRHLGVPTVTVPMGVMADIGMPVGLTFAGRAYDD
STLLRLASAFEATGTKRLIPPRTPVLRK
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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