SitesBLAST
Comparing WP_013538388.1 NCBI__GCF_000185805.1:WP_013538388.1 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)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
62% identity, 98% coverage: 3:480/487 of query aligns to 2:470/478 of 3h0mA
- active site: K72 (= K81), S147 (= S156), S148 (= S157), S166 (= S175), T168 (= T177), G169 (= G178), G170 (= G179), S171 (= S180), Q174 (= Q183)
- binding glutamine: M122 (= M131), G123 (= G132), D167 (= D176), T168 (= T177), G169 (= G178), G170 (= G179), S171 (= S180), F199 (= F208), Y302 (= Y311), R351 (= R360), D418 (= D427)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
62% identity, 98% coverage: 3:480/487 of query aligns to 2:470/478 of 3h0lA
- active site: K72 (= K81), S147 (= S156), S148 (= S157), S166 (= S175), T168 (= T177), G169 (= G178), G170 (= G179), S171 (= S180), Q174 (= Q183)
- binding asparagine: G123 (= G132), S147 (= S156), G169 (= G178), G170 (= G179), S171 (= S180), Y302 (= Y311), R351 (= R360), D418 (= D427)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
55% identity, 99% coverage: 1:481/487 of query aligns to 1:478/485 of 2f2aA
- active site: K79 (= K81), S154 (= S156), S155 (= S157), S173 (= S175), T175 (= T177), G176 (= G178), G177 (= G179), S178 (= S180), Q181 (= Q183)
- binding glutamine: G130 (= G132), S154 (= S156), D174 (= D176), T175 (= T177), G176 (= G178), S178 (= S180), F206 (= F208), Y309 (= Y311), Y310 (= Y312), R358 (= R360), D425 (= D427)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
55% identity, 99% coverage: 1:481/487 of query aligns to 1:478/485 of 2dqnA
- active site: K79 (= K81), S154 (= S156), S155 (= S157), S173 (= S175), T175 (= T177), G176 (= G178), G177 (= G179), S178 (= S180), Q181 (= Q183)
- binding asparagine: M129 (= M131), G130 (= G132), T175 (= T177), G176 (= G178), S178 (= S180), Y309 (= Y311), Y310 (= Y312), R358 (= R360), D425 (= D427)
3kfuE Crystal structure of the transamidosome (see paper)
49% identity, 96% coverage: 9:476/487 of query aligns to 3:454/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
37% identity, 83% coverage: 73:475/487 of query aligns to 30:449/450 of 4n0iA
- active site: K38 (= K81), S116 (= S156), S117 (= S157), T135 (≠ S175), T137 (= T177), G138 (= G178), G139 (= G179), S140 (= S180), L143 (≠ Q183)
- binding glutamine: G89 (= G132), T137 (= T177), G138 (= G178), S140 (= S180), Y168 (≠ F208), Y271 (= Y311), Y272 (= Y312), R320 (= R360), D404 (= D427)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
35% identity, 83% coverage: 73:476/487 of query aligns to 87:497/508 of 3a1iA
- active site: K95 (= K81), S170 (= S156), S171 (= S157), G189 (≠ S175), Q191 (≠ T177), G192 (= G178), G193 (= G179), A194 (≠ S180), I197 (≠ Q183)
- binding benzamide: F145 (≠ M131), S146 (≠ G132), G147 (≠ S133), Q191 (≠ T177), G192 (= G178), G193 (= G179), A194 (≠ S180), W327 (≠ Y311)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
33% identity, 97% coverage: 5:476/487 of query aligns to 5:476/487 of 1m21A
- active site: K81 (= K81), S160 (= S156), S161 (= S157), T179 (≠ S175), T181 (= T177), D182 (≠ G178), G183 (= G179), S184 (= S180), C187 (≠ Q183)
- binding : A129 (= A130), N130 (vs. gap), F131 (vs. gap), C158 (≠ G154), G159 (= G155), S160 (= S156), S184 (= S180), C187 (≠ Q183), I212 (≠ F208), R318 (≠ Y312), L321 (≠ A315), L365 (≠ M362), F426 (vs. gap)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
32% identity, 99% coverage: 2:485/487 of query aligns to 24:496/507 of Q84DC4
- T31 (≠ K9) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K81) mutation to A: Abolishes activity on mandelamide.
- S180 (= S156) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S157) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G178) 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 (= S180) mutation to A: Abolishes activity on mandelamide.
- Q207 (= Q183) 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 (= S307) 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 (≠ D374) 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 (≠ A432) 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.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
31% identity, 90% coverage: 50:487/487 of query aligns to 173:599/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A130), T258 (≠ S133), S281 (= S156), G302 (≠ T177), G303 (= G178), S305 (= S180), S472 (≠ T365), I532 (vs. gap), M539 (≠ I421)
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)
31% identity, 90% coverage: 50:487/487 of query aligns to 173:599/607 of Q7XJJ7
- K205 (= K81) mutation to A: Loss of activity.
- SS 281:282 (= SS 156:157) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 177:180) binding
- S305 (= S180) mutation to A: Loss of activity.
- R307 (= R182) mutation to A: Loss of activity.
- S360 (≠ L235) mutation to A: No effect.
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
31% identity, 93% coverage: 24:476/487 of query aligns to 19:448/457 of 6c6gA
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
29% identity, 97% coverage: 6:476/487 of query aligns to 6:473/490 of 4yjiA
- active site: K79 (= K81), S158 (= S156), S159 (= S157), G179 (≠ T177), G180 (= G178), G181 (= G179), A182 (≠ S180)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ N83), G132 (≠ A130), S158 (= S156), G179 (≠ T177), G180 (= G178), A182 (≠ S180)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
28% identity, 96% coverage: 10:476/487 of query aligns to 9:444/457 of 5h6sC
- active site: K77 (= K81), S152 (= S156), S153 (= S157), L173 (≠ T177), G174 (= G178), G175 (= G179), S176 (= S180)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A130), R128 (≠ G132), W129 (≠ S133), S152 (= S156), L173 (≠ T177), G174 (= G178), S176 (= S180), W306 (≠ Y311), F338 (≠ Y345)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
31% identity, 86% coverage: 55:475/487 of query aligns to 66:460/605 of Q936X2
- K91 (= K81) mutation to A: Loss of activity.
- S165 (= S156) mutation to A: Loss of activity.
- S189 (= S180) mutation to A: Loss of activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
33% identity, 84% coverage: 73:479/487 of query aligns to 64:441/461 of 4gysB
- active site: K72 (= K81), S146 (= S156), S147 (= S157), T165 (≠ S175), T167 (= T177), A168 (≠ G178), G169 (= G179), S170 (= S180), V173 (≠ Q183)
- binding malonate ion: A120 (= A130), G122 (= G132), S146 (= S156), T167 (= T177), A168 (≠ G178), S170 (= S180), S193 (≠ Y203), G194 (= G204), V195 (≠ L205), R200 (≠ S210), Y297 (≠ F326), R305 (≠ N337)
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)
43% identity, 31% coverage: 73:221/487 of query aligns to 28:178/425 of Q9FR37
- K36 (= K81) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S156) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S157) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D176) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S180) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C188) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 214 S→T: Slightly reduces catalytic activity.
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
32% identity, 52% coverage: 14:265/487 of query aligns to 13:259/482 of 3a2qA
- active site: K69 (= K81), S147 (= S156), S148 (= S157), N166 (≠ S175), A168 (≠ T177), A169 (≠ G178), G170 (= G179), A171 (≠ S180), I174 (≠ Q183)
- binding 6-aminohexanoic acid: G121 (≠ A130), G121 (≠ A130), N122 (≠ M131), S147 (= S156), A168 (≠ T177), A168 (≠ T177), A169 (≠ G178), A171 (≠ S180)
Sites not aligning to the query:
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)
28% identity, 61% coverage: 3:297/487 of query aligns to 74:361/579 of Q9TUI8
- S217 (= S156) mutation to A: Loss of activity.
- S218 (= S157) mutation to A: Lowers activity by at least 98%.
- D237 (= D176) mutation D->E,N: Loss of activity.
- S241 (= S180) mutation to A: Loss of activity.
- C249 (= C188) mutation to A: Loss of activity.
3qkvA Crystal structure of fatty acid amide hydrolase with small molecule compound (see paper)
32% identity, 49% coverage: 73:309/487 of query aligns to 106:345/549 of 3qkvA
- active site: K114 (= K81), S189 (= S156), S190 (= S157), T208 (≠ S175), I210 (≠ T177), G211 (= G178), G212 (= G179), S213 (= S180), F216 (≠ Q183)
- binding (6-bromo-1'H,4H-spiro[1,3-benzodioxine-2,4'-piperidin]-1'-yl)methanol: L164 (≠ M131), S165 (≠ G132), I210 (≠ T177), G211 (= G178), S213 (= S180)
Sites not aligning to the query:
Query Sequence
>WP_013538388.1 NCBI__GCF_000185805.1:WP_013538388.1
MELLEKSLKELHTLIKKKELKPSELVQANIERIEQTEEKLNAYITVCAQEALEKAKVADE
ELLRLSEDEIPELFGIPIAIKDNINVEGIRMTCASRMLESFISPYDATVTKKLRERGAIF
IGKNNLDEFAMGSSTETSYFGPTKNPWDFSRVPGGSSGGSAAAVAARSALASLGSDTGGS
IRQPAAFCGVVGLKPTYGRVSRYGLTAFASSLDQIGPITKNVEDAAYLLNIISGLDSKDA
TSAKLPVPNFLEALNGEVKGLKVGLPKEYFVEGIEPEVKALVEEAARKLEKLGAELVEVS
LPTTKYSVETYYIIAPAEASSNLGRFDGVRYTYRAKNYKGLVDMYCKTRAEGFGDEVKRR
IMIGTYTLSAGYYDAYYLKAQKVRTLIYNDFQKAFESVDVLLTPVTPEVAFKIGEKTDDP
IKMYLSDVFTIAVNLAGLPALSLPCGLTAQNLPVGVQLIGKAFDEETILKVAHALEAELN
LSLKPAL
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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