SitesBLAST
Comparing WP_011765689.1 NCBI__GCF_000061505.1:WP_011765689.1 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)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
29% identity, 98% coverage: 8:465/465 of query aligns to 3:485/485 of 2f2aA
- active site: K79 (= K84), S154 (= S157), S155 (= S158), S173 (≠ T176), T175 (= T178), G176 (= G179), G177 (= G180), S178 (= S181), Q181 (≠ F184)
- binding glutamine: G130 (vs. gap), S154 (= S157), D174 (= D177), T175 (= T178), G176 (= G179), S178 (= S181), F206 (≠ L209), Y309 (≠ W303), Y310 (≠ P304), R358 (≠ L339), D425 (≠ I404)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
29% identity, 98% coverage: 8:465/465 of query aligns to 3:485/485 of 2dqnA
- active site: K79 (= K84), S154 (= S157), S155 (= S158), S173 (≠ T176), T175 (= T178), G176 (= G179), G177 (= G180), S178 (= S181), Q181 (≠ F184)
- binding asparagine: M129 (≠ F134), G130 (vs. gap), T175 (= T178), G176 (= G179), S178 (= S181), Y309 (≠ W303), Y310 (≠ P304), R358 (≠ L339), D425 (≠ I404)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
31% identity, 96% coverage: 13:460/465 of query aligns to 7:474/478 of 3h0mA
- active site: K72 (= K84), S147 (= S157), S148 (= S158), S166 (≠ T176), T168 (= T178), G169 (= G179), G170 (= G180), S171 (= S181), Q174 (≠ F184)
- binding glutamine: M122 (≠ F134), G123 (vs. gap), D167 (= D177), T168 (= T178), G169 (= G179), G170 (= G180), S171 (= S181), F199 (≠ L209), Y302 (≠ W309), R351 (≠ L339), D418 (≠ L403)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
31% identity, 96% coverage: 13:460/465 of query aligns to 7:474/478 of 3h0lA
- active site: K72 (= K84), S147 (= S157), S148 (= S158), S166 (≠ T176), T168 (= T178), G169 (= G179), G170 (= G180), S171 (= S181), Q174 (≠ F184)
- binding asparagine: G123 (vs. gap), S147 (= S157), G169 (= G179), G170 (= G180), S171 (= S181), Y302 (≠ W309), R351 (≠ L339), D418 (≠ L403)
3kfuE Crystal structure of the transamidosome (see paper)
37% identity, 95% coverage: 23:462/465 of query aligns to 12:461/468 of 3kfuE
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
29% identity, 96% coverage: 8:455/465 of query aligns to 126:590/607 of Q7XJJ7
- K205 (= K84) mutation to A: Loss of activity.
- SS 281:282 (= SS 157:158) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 178:181) binding
- S305 (= S181) mutation to A: Loss of activity.
- R307 (= R183) mutation to A: Loss of activity.
- S360 (≠ P236) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
29% identity, 96% coverage: 8:455/465 of query aligns to 126:590/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A133), T258 (= T136), S281 (= S157), G302 (≠ T178), G303 (= G179), S305 (= S181), S472 (≠ A335), I532 (≠ P397), M539 (≠ I404)
Sites not aligning to the query:
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
33% identity, 95% coverage: 11:453/465 of query aligns to 1:448/457 of 6c6gA
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
34% identity, 97% coverage: 12:464/465 of query aligns to 7:485/487 of 1m21A
- active site: K81 (= K84), S160 (= S157), S161 (= S158), T179 (= T176), T181 (= T178), D182 (≠ G179), G183 (= G180), S184 (= S181), C187 (≠ F184)
- binding : A129 (= A133), N130 (≠ F134), F131 (≠ A135), C158 (≠ G155), G159 (≠ A156), S160 (= S157), S184 (= S181), C187 (≠ F184), I212 (≠ L209), R318 (vs. gap), L321 (vs. gap), L365 (= L336), F426 (≠ L393)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
30% identity, 96% coverage: 11:455/465 of query aligns to 28:489/507 of Q84DC4
- T31 (≠ A14) 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 (= S159) mutation to A: Significantly decreases activity on mandelamide.
- S181 (≠ G160) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G179) 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 (= S181) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ F184) 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 (≠ A306) 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 (≠ R353) 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 (= I404) 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.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
34% identity, 82% coverage: 54:436/465 of query aligns to 45:421/461 of 4gysB
- active site: K72 (= K84), S146 (= S157), S147 (= S158), T165 (= T176), T167 (= T178), A168 (≠ G179), G169 (= G180), S170 (= S181), V173 (≠ F184)
- binding malonate ion: A120 (≠ T130), G122 (= G132), S146 (= S157), T167 (= T178), A168 (≠ G179), S170 (= S181), S193 (≠ H204), G194 (= G205), V195 (= V206), R200 (≠ P211), Y297 (≠ C313), R305 (≠ A318)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
31% identity, 82% coverage: 74:455/465 of query aligns to 85:499/508 of 3a1iA
- active site: K95 (= K84), S170 (= S157), S171 (= S158), G189 (≠ T176), Q191 (≠ T178), G192 (= G179), G193 (= G180), A194 (≠ S181), I197 (≠ F184)
- binding benzamide: F145 (= F134), S146 (≠ A135), G147 (vs. gap), Q191 (≠ T178), G192 (= G179), G193 (= G180), A194 (≠ S181), W327 (= W303)
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
27% identity, 83% coverage: 59:446/465 of query aligns to 10:443/450 of 4n0iA
- active site: K38 (= K84), S116 (= S157), S117 (= S158), T135 (= T176), T137 (= T178), G138 (= G179), G139 (= G180), S140 (= S181), L143 (≠ F184)
- binding glutamine: G89 (vs. gap), T137 (= T178), G138 (= G179), S140 (= S181), Y168 (≠ L209), Y271 (≠ W309), Y272 (≠ E310), R320 (≠ L339), D404 (≠ I404)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
28% identity, 98% coverage: 8:462/465 of query aligns to 3:482/490 of 4yjiA
- active site: K79 (= K84), S158 (= S157), S159 (= S158), G179 (≠ T178), G180 (= G179), G181 (= G180), A182 (≠ S181)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L86), G132 (≠ A133), S158 (= S157), G179 (≠ T178), G180 (= G179), A182 (≠ S181)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
30% identity, 95% coverage: 11:453/465 of query aligns to 2:407/412 of 1ocmA
- active site: K62 (= K84), S131 (= S157), S132 (= S158), T152 (= T178), G153 (= G179), G154 (= G180), S155 (= S181)
- binding pyrophosphate 2-: R113 (≠ P137), S131 (= S157), Q151 (≠ D177), T152 (= T178), G153 (= G179), G154 (= G180), S155 (= S181), R158 (≠ F184), P359 (= P397)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
30% identity, 95% coverage: 11:453/465 of query aligns to 2:407/412 of 1o9oA
- active site: K62 (= K84), A131 (≠ S157), S132 (= S158), T150 (= T176), T152 (= T178), G153 (= G179), G154 (= G180), S155 (= S181), R158 (≠ F184)
- binding 3-amino-3-oxopropanoic acid: G130 (≠ A156), T152 (= T178), G153 (= G179), G154 (= G180), S155 (= S181), R158 (≠ F184), P359 (= P397)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
28% identity, 96% coverage: 7:453/465 of query aligns to 1:444/457 of 5h6sC
- active site: K77 (= K84), S152 (= S157), S153 (= S158), L173 (≠ T178), G174 (= G179), G175 (= G180), S176 (= S181)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A142), R128 (vs. gap), W129 (vs. gap), S152 (= S157), L173 (≠ T178), G174 (= G179), S176 (= S181), W306 (= W309), F338 (≠ H352)
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
35% identity, 50% coverage: 7:238/465 of query aligns to 1:241/564 of 6te4A
Sites not aligning to the query:
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
30% identity, 81% coverage: 75:452/465 of query aligns to 82:460/605 of Q936X2
- K91 (= K84) mutation to A: Loss of activity.
- S165 (= S157) mutation to A: Loss of activity.
- S189 (= S181) mutation to A: Loss of activity.
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
36% identity, 53% coverage: 17:263/465 of query aligns to 11:259/482 of 3a2qA
- active site: K69 (= K84), S147 (= S157), S148 (= S158), N166 (≠ T176), A168 (≠ T178), A169 (≠ G179), G170 (= G180), A171 (≠ S181), I174 (≠ F184)
- binding 6-aminohexanoic acid: G121 (= G132), G121 (= G132), N122 (≠ A133), S147 (= S157), A168 (≠ T178), A168 (≠ T178), A169 (≠ G179), A171 (≠ S181)
Sites not aligning to the query:
Query Sequence
>WP_011765689.1 NCBI__GCF_000061505.1:WP_011765689.1
MSRTAPELHYLEIAELAPLLRAGDISPLALTRHMLARIDALDSRLHAYARVTADEALAAA
AQAEADIAAGRYRGPLHGVPVAVKDLFWTRGTVTACGTTVLADFVPDEDATVVRRLREAG
AVILGKLQMTEGAFATPHPDLAAPLNPWGADHWTGASSSGSGVATAAGLCFAALGTDTGG
SIRFPAAANGLSGLKPGWGRVSRHGVFPLAPTLDHVGPMARSVRDVALMYQAIAGPDPLD
PTSLDDAPRAAGHSGLAGLRVGIDAAWNARGSDAEVLAGCARLREALVAGGAEIVELELP
ESWPIAGAWELLCGVQTAVAHAATYPARAADYGPALARLIEVGRAAGAMDYHRAQLAALD
FGGRLERALAGVDLLLAPVQPFAAPTHARLGELAQSPELNQRLIQFTAPLNISGSPSLAL
PCGSTAAGLPVGCQLIARKGGEATLLAAGAALQAVTHWHRAHPPL
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