SitesBLAST
Comparing WP_015818617.1 NCBI__GCF_000023025.1:WP_015818617.1 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)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
48% identity, 92% coverage: 24:451/463 of query aligns to 22:452/457 of 6c6gA
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
32% identity, 97% coverage: 5:451/463 of query aligns to 7:469/478 of 3h0mA
- active site: K72 (= K74), S147 (= S150), S148 (= S151), S166 (= S169), T168 (= T171), G169 (≠ N172), G170 (= G173), S171 (= S174), Q174 (≠ V177)
- binding glutamine: M122 (≠ Y125), G123 (≠ D126), D167 (= D170), T168 (= T171), G169 (≠ N172), G170 (= G173), S171 (= S174), F199 (= F202), Y302 (≠ A301), R351 (= R331), D418 (vs. gap)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
32% identity, 97% coverage: 5:451/463 of query aligns to 7:469/478 of 3h0lA
- active site: K72 (= K74), S147 (= S150), S148 (= S151), S166 (= S169), T168 (= T171), G169 (≠ N172), G170 (= G173), S171 (= S174), Q174 (≠ V177)
- binding asparagine: G123 (≠ D126), S147 (= S150), G169 (≠ N172), G170 (= G173), S171 (= S174), Y302 (≠ A301), R351 (= R331), D418 (vs. gap)
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
33% identity, 90% coverage: 34:448/463 of query aligns to 166:589/607 of Q7XJJ7
- K205 (= K74) mutation to A: Loss of activity.
- SS 281:282 (= SS 150:151) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TNGS 171:174) binding substrate
- S305 (= S174) mutation to A: Loss of activity.
- R307 (= R176) mutation to A: Loss of activity.
- S360 (≠ Y229) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
33% identity, 90% coverage: 34:448/463 of query aligns to 166:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A124), T258 (≠ F127), S281 (= S150), G302 (≠ T171), G303 (≠ N172), S305 (= S174), S472 (≠ R331), I532 (≠ Q391), M539 (≠ G398)
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
33% identity, 90% coverage: 34:448/463 of query aligns to 166:589/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A124), G302 (≠ T171), G303 (≠ N172), G304 (= G173), A305 (≠ S174), V442 (≠ L303), I475 (≠ A334), M539 (≠ G398)
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
33% identity, 90% coverage: 34:448/463 of query aligns to 166:589/605 of 8ey1D
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
31% identity, 94% coverage: 15:447/463 of query aligns to 21:473/485 of 2f2aA
- active site: K79 (= K74), S154 (= S150), S155 (= S151), S173 (= S169), T175 (= T171), G176 (≠ N172), G177 (= G173), S178 (= S174), Q181 (≠ V177)
- binding glutamine: G130 (≠ D126), S154 (= S150), D174 (= D170), T175 (= T171), G176 (≠ N172), S178 (= S174), F206 (= F202), Y309 (≠ A301), Y310 (= Y302), R358 (= R331), D425 (≠ G398)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
31% identity, 94% coverage: 15:447/463 of query aligns to 21:473/485 of 2dqnA
- active site: K79 (= K74), S154 (= S150), S155 (= S151), S173 (= S169), T175 (= T171), G176 (≠ N172), G177 (= G173), S178 (= S174), Q181 (≠ V177)
- binding asparagine: M129 (≠ Y125), G130 (≠ D126), T175 (= T171), G176 (≠ N172), S178 (= S174), Y309 (≠ A301), Y310 (= Y302), R358 (= R331), D425 (≠ G398)
3kfuE Crystal structure of the transamidosome (see paper)
32% identity, 96% coverage: 6:449/463 of query aligns to 3:456/468 of 3kfuE
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)
50% identity, 35% coverage: 66:226/463 of query aligns to 28:189/425 of Q9FR37
- K36 (= K74) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S150) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S151) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D170) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S174) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C182) 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)
30% identity, 84% coverage: 66:456/463 of query aligns to 87:506/508 of 3a1iA
- active site: K95 (= K74), S170 (= S150), S171 (= S151), G189 (≠ S169), Q191 (≠ T171), G192 (≠ N172), G193 (= G173), A194 (≠ S174), I197 (≠ V177)
- binding benzamide: F145 (≠ Y125), S146 (≠ D126), G147 (≠ F127), Q191 (≠ T171), G192 (≠ N172), G193 (= G173), A194 (≠ S174), W327 (≠ E292)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
30% identity, 92% coverage: 23:449/463 of query aligns to 25:470/482 of 3a2qA
- active site: K69 (= K74), S147 (= S150), S148 (= S151), N166 (≠ S169), A168 (≠ T171), A169 (≠ N172), G170 (= G173), A171 (≠ S174), I174 (≠ V177)
- binding 6-aminohexanoic acid: G121 (≠ A124), G121 (≠ A124), N122 (≠ Y125), S147 (= S150), A168 (≠ T171), A168 (≠ T171), A169 (≠ N172), A171 (≠ S174), C313 (≠ S310)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
29% identity, 94% coverage: 1:437/463 of query aligns to 1:428/461 of 4gysB
- active site: K72 (= K74), S146 (= S150), S147 (= S151), T165 (≠ S169), T167 (= T171), A168 (≠ N172), G169 (= G173), S170 (= S174), V173 (= V177)
- binding malonate ion: A120 (= A124), G122 (≠ D126), S146 (= S150), T167 (= T171), A168 (≠ N172), S170 (= S174), S193 (≠ T197), G194 (= G198), V195 (≠ T199), R200 (≠ D204), Y297 (vs. gap), R305 (≠ N306)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
37% identity, 47% coverage: 18:236/463 of query aligns to 24:246/487 of 1m21A
- active site: K81 (= K74), S160 (= S150), S161 (= S151), T179 (≠ S169), T181 (= T171), D182 (≠ N172), G183 (= G173), S184 (= S174), C187 (≠ V177)
- binding : A129 (= A124), N130 (≠ Y125), F131 (vs. gap), C158 (≠ G148), G159 (= G149), S160 (= S150), S184 (= S174), C187 (≠ V177), I212 (≠ F202)
Sites not aligning to the query:
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
28% identity, 96% coverage: 5:447/463 of query aligns to 30:487/507 of Q84DC4
- T31 (≠ N6) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K74) mutation to A: Abolishes activity on mandelamide.
- S180 (= S150) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S151) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ N172) 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 (= S174) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ V177) 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 (≠ L283) 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 (≠ A340) 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 (≠ L393) 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.
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
28% identity, 80% coverage: 6:377/463 of query aligns to 8:384/457 of 5h6sC
- active site: K77 (= K74), S152 (= S150), S153 (= S151), L173 (≠ T171), G174 (≠ N172), G175 (= G173), S176 (= S174)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A124), R128 (≠ D126), W129 (≠ F127), S152 (= S150), L173 (≠ T171), G174 (≠ N172), S176 (= S174), W306 (≠ I304), F338 (= F332)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
30% identity, 79% coverage: 64:430/463 of query aligns to 81:444/605 of Q936X2
- K91 (= K74) mutation to A: Loss of activity.
- S165 (= S150) mutation to A: Loss of activity.
- S189 (= S174) mutation to A: Loss of activity.
Q9MUK5 Translocon at the outer membrane of chloroplasts 64 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
45% identity, 34% coverage: 71:226/463 of query aligns to 66:222/593 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.
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
28% identity, 79% coverage: 66:431/463 of query aligns to 30:434/450 of 4n0iA
- active site: K38 (= K74), S116 (= S150), S117 (= S151), T135 (≠ S169), T137 (= T171), G138 (≠ N172), G139 (= G173), S140 (= S174), L143 (≠ V177)
- binding glutamine: G89 (≠ D126), T137 (= T171), G138 (≠ N172), S140 (= S174), Y168 (≠ F202), Y271 (vs. gap), Y272 (= Y302), R320 (= R331), D404 (vs. gap)
Query Sequence
>WP_015818617.1 NCBI__GCF_000023025.1:WP_015818617.1
MTGHLNEIQAFYAENPLNIVQNIEQQLDTIVQINPSLNAFTSISRRRAIEAAERLTEKQN
LAEMPLAGATFAVKNLFDIAGEVTLAGSKLNERHSPASQDATLIERLENAGAILTGALNM
GEYAYDFTGENCHHGNCGNPYKLDHMAGGSSSGSAAAVAAGLVDFSLGSDTNGSIRVPAS
FCGIFGLKPTYGRLPRTGTFPFSDSLDHLGPLARSTQDLARVYDVLQGYDGGDHACVDRH
SSHTVSQLNLGIQHLRFARLEGYFNCEHFPQARSAMDKVCKALDVQEEIVPEGVTEGRSA
AYLITNIEGSSLHLSRLQQNAEEFDPDTRDRFLAGAMLPAAWYIRAQQVRRWYQEKMLAL
FKNVEVLIAPATPCVAPKQGQKTLKIAGEEQLLRPNLGYFTQPFSAIGLPSIVVPTQDDE
TGMPIGIQIIAAPWREDICLRVAAYLEDAGFCFVPPPLYSSAA
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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