SitesBLAST
Comparing WP_086511931.1 NCBI__GCF_002151265.1:WP_086511931.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
35% identity, 98% coverage: 9:498/502 of query aligns to 5:480/482 of 3a2qA
- active site: K69 (= K75), S147 (= S151), S148 (= S152), N166 (≠ G170), A168 (≠ G172), A169 (≠ G173), G170 (= G174), A171 (≠ S175), I174 (= I178)
- binding 6-aminohexanoic acid: G121 (= G125), G121 (= G125), N122 (≠ L126), S147 (= S151), A168 (≠ G172), A168 (≠ G172), A169 (≠ G173), A171 (≠ S175), C313 (≠ A322)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
29% identity, 96% coverage: 14:494/502 of query aligns to 11:481/490 of 4yjiA
- active site: K79 (= K75), S158 (= S151), S159 (= S152), G179 (= G172), G180 (= G173), G181 (= G174), A182 (≠ S175)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L77), G132 (= G125), S158 (= S151), G179 (= G172), G180 (= G173), A182 (≠ S175)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 96% coverage: 14:496/502 of query aligns to 10:476/478 of 3h0mA
- active site: K72 (= K75), S147 (= S151), S148 (= S152), S166 (≠ G170), T168 (≠ G172), G169 (= G173), G170 (= G174), S171 (= S175), Q174 (≠ I178)
- binding glutamine: M122 (≠ L126), G123 (≠ M127), D167 (= D171), T168 (≠ G172), G169 (= G173), G170 (= G174), S171 (= S175), F199 (≠ R206), Y302 (≠ L315), R351 (= R379), D418 (≠ T437)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 96% coverage: 14:496/502 of query aligns to 10:476/478 of 3h0lA
- active site: K72 (= K75), S147 (= S151), S148 (= S152), S166 (≠ G170), T168 (≠ G172), G169 (= G173), G170 (= G174), S171 (= S175), Q174 (≠ I178)
- binding asparagine: G123 (≠ M127), S147 (= S151), G169 (= G173), G170 (= G174), S171 (= S175), Y302 (≠ L315), R351 (= R379), D418 (≠ T437)
3kfuE Crystal structure of the transamidosome (see paper)
33% identity, 95% coverage: 18:495/502 of query aligns to 9:462/468 of 3kfuE
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
28% identity, 96% coverage: 13:494/502 of query aligns to 10:479/485 of 2f2aA
- active site: K79 (= K75), S154 (= S151), S155 (= S152), S173 (≠ G170), T175 (≠ G172), G176 (= G173), G177 (= G174), S178 (= S175), Q181 (≠ I178)
- binding glutamine: G130 (≠ M127), S154 (= S151), D174 (= D171), T175 (≠ G172), G176 (= G173), S178 (= S175), F206 (≠ R206), Y309 (vs. gap), Y310 (vs. gap), R358 (≠ L338), D425 (≠ A409)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
28% identity, 96% coverage: 13:494/502 of query aligns to 10:479/485 of 2dqnA
- active site: K79 (= K75), S154 (= S151), S155 (= S152), S173 (≠ G170), T175 (≠ G172), G176 (= G173), G177 (= G174), S178 (= S175), Q181 (≠ I178)
- binding asparagine: M129 (≠ L126), G130 (≠ M127), T175 (≠ G172), G176 (= G173), S178 (= S175), Y309 (vs. gap), Y310 (vs. gap), R358 (≠ L338), D425 (≠ A409)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
26% identity, 96% coverage: 18:498/502 of query aligns to 14:450/457 of 5h6sC
- active site: K77 (= K75), S152 (= S151), S153 (= S152), L173 (≠ G172), G174 (= G173), G175 (= G174), S176 (= S175)
- binding 4-oxidanylbenzohydrazide: C126 (≠ G125), R128 (≠ M127), W129 (≠ G128), S152 (= S151), L173 (≠ G172), G174 (= G173), S176 (= S175), W306 (≠ D304), F338 (≠ E341)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
27% identity, 87% coverage: 50:486/502 of query aligns to 187:588/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (= G125), T258 (≠ G128), S281 (= S151), G302 (= G172), G303 (= G173), S305 (= S175), S472 (≠ I347), I532 (≠ Q428), M539 (≠ S435)
Sites not aligning to the query:
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
29% identity, 81% coverage: 79:486/502 of query aligns to 98:497/508 of 3a1iA
- active site: S170 (= S151), S171 (= S152), G189 (= G170), Q191 (≠ G172), G192 (= G173), G193 (= G174), A194 (≠ S175), I197 (= I178)
- binding benzamide: F145 (≠ L126), S146 (≠ M127), G147 (= G128), Q191 (≠ G172), G192 (= G173), G193 (= G174), A194 (≠ S175), W327 (vs. gap)
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)
27% identity, 87% coverage: 50:486/502 of query aligns to 187:588/607 of Q7XJJ7
- K205 (= K75) mutation to A: Loss of activity.
- SS 281:282 (= SS 151:152) mutation to AA: Loss of activity.
- GGGS 302:305 (= GGGS 172:175) binding
- S305 (= S175) mutation to A: Loss of activity.
- R307 (= R177) mutation to A: Loss of activity.
- S360 (≠ M231) mutation to A: No effect.
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
33% identity, 42% coverage: 27:236/502 of query aligns to 27:244/487 of 1m21A
- active site: K81 (= K75), S160 (= S151), S161 (= S152), T179 (≠ G170), T181 (≠ G172), D182 (≠ G173), G183 (= G174), S184 (= S175), C187 (≠ I178)
- binding : A129 (≠ L124), N130 (≠ G125), F131 (≠ L126), C158 (≠ G149), G159 (= G150), S160 (= S151), S184 (= S175), C187 (≠ I178), I212 (≠ V204)
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)
39% identity, 26% coverage: 67:195/502 of query aligns to 28:157/425 of Q9FR37
- K36 (= K75) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S151) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S152) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D171) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S175) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C183) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 214 S→T: Slightly reduces catalytic activity.
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
28% identity, 95% coverage: 12:486/502 of query aligns to 2:407/412 of 1o9oA
- active site: K62 (= K75), A131 (≠ S151), S132 (= S152), T150 (≠ G170), T152 (≠ G172), G153 (= G173), G154 (= G174), S155 (= S175), R158 (≠ I178)
- binding 3-amino-3-oxopropanoic acid: G130 (= G150), T152 (≠ G172), G153 (= G173), G154 (= G174), S155 (= S175), R158 (≠ I178), P359 (= P417)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
28% identity, 95% coverage: 12:486/502 of query aligns to 2:407/412 of 1ocmA
- active site: K62 (= K75), S131 (= S151), S132 (= S152), T152 (≠ G172), G153 (= G173), G154 (= G174), S155 (= S175)
- binding pyrophosphate 2-: R113 (≠ T130), S131 (= S151), Q151 (≠ D171), T152 (≠ G172), G153 (= G173), G154 (= G174), S155 (= S175), R158 (≠ I178), P359 (= P417)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
36% identity, 36% coverage: 14:195/502 of query aligns to 6:194/457 of 6c6gA
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)
27% identity, 56% coverage: 14:296/502 of query aligns to 82:360/579 of Q9TUI8
- S217 (= S151) mutation to A: Loss of activity.
- S218 (= S152) mutation to A: Lowers activity by at least 98%.
- D237 (= D171) mutation D->E,N: Loss of activity.
- S241 (= S175) mutation to A: Loss of activity.
- C249 (= C183) mutation to A: Loss of activity.
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
27% identity, 81% coverage: 66:470/502 of query aligns to 82:445/605 of Q936X2
- K91 (= K75) mutation to A: Loss of activity.
- S165 (= S151) mutation to A: Loss of activity.
- S189 (= S175) mutation to A: Loss of activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
26% identity, 86% coverage: 52:485/502 of query aligns to 45:437/461 of 4gysB
- active site: K72 (= K75), S146 (= S151), S147 (= S152), T165 (≠ G170), T167 (≠ G172), A168 (≠ G173), G169 (= G174), S170 (= S175), V173 (≠ I178)
- binding malonate ion: A120 (vs. gap), G122 (= G125), S146 (= S151), T167 (≠ G172), A168 (≠ G173), S170 (= S175), S193 (≠ G198), G194 (≠ P199), V195 (≠ L200), R200 (= R206), Y297 (= Y316), R305 (≠ E330)
1mt5A Crystal structure of fatty acid amide hydrolase (see paper)
28% identity, 48% coverage: 56:296/502 of query aligns to 83:324/537 of 1mt5A
- active site: K106 (= K75), S181 (= S151), S182 (= S152), T200 (≠ G170), I202 (≠ G172), G203 (= G173), G204 (= G174), S205 (= S175), F208 (≠ I178)
- binding methyl arachidonyl fluorophosphonate: M155 (≠ G125), L156 (= L126), S157 (≠ M127), S181 (= S151), D201 (= D171), I202 (≠ G172), G203 (= G173), S205 (= S175)
Sites not aligning to the query:
Query Sequence
>WP_086511931.1 NCBI__GCF_002151265.1:WP_086511931.1
MDIEEYRRHDGMGLAELIRRGEVSRGEVFAAACAAIERDNPHLRALVRTRFERARSEAES
VDPEAPLAGVPTLTKDLLMALEGEPLAFGSAALAEWKAPVESTLVARVREAGLAILGQTA
TPELGLMGITEPRAFPHPVNPWNAEHSPGGSSGGAAAAVAGGLVPLAMAGDGGGSIRIPA
AYCGLFGLKPSRGRVPQGPLHGEVWRGAVVEHAVTRSVRDSAALLEAINGMDEGGPYPVP
RERGFLAALERPPEPLRIAVSLGEPLSKPLGTRLDPEVRLAVEGAARTLEGLGHHLEWAD
PPVDGERLANAYLTLYLGHVTADLAWISRETGVPVSRLDIEPSTRAIARLGQHLPVRDYE
LAKRDWNAAARAMGAFHRRFDVLLMPVTAAPAPRLGELYPPAWQQRLMALLAIPGLPRLA
LKAGMLGQLARDALSRTPYTQLANLTGQPAMSLPLHVTPQGLPVGVQVVGSMGDERRLLA
LAAQLEAEVQWQRHLPRVAQGG
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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