SitesBLAST
Comparing WP_068460249.1 NCBI__GCF_001541235.1:WP_068460249.1 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)
51% identity, 94% coverage: 16:483/500 of query aligns to 15:473/485 of 2f2aA
- active site: K79 (= K79), S154 (= S164), S155 (= S165), S173 (≠ T183), T175 (= T185), G176 (= G186), G177 (= G187), S178 (= S188), Q181 (= Q191)
- binding glutamine: G130 (= G130), S154 (= S164), D174 (= D184), T175 (= T185), G176 (= G186), S178 (= S188), F206 (= F216), Y309 (= Y319), Y310 (= Y320), R358 (= R367), D425 (= D434)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
51% identity, 94% coverage: 16:483/500 of query aligns to 15:473/485 of 2dqnA
- active site: K79 (= K79), S154 (= S164), S155 (= S165), S173 (≠ T183), T175 (= T185), G176 (= G186), G177 (= G187), S178 (= S188), Q181 (= Q191)
- binding asparagine: M129 (= M129), G130 (= G130), T175 (= T185), G176 (= G186), S178 (= S188), Y309 (= Y319), Y310 (= Y320), R358 (= R367), D425 (= D434)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
48% identity, 98% coverage: 4:492/500 of query aligns to 2:476/478 of 3h0mA
- active site: K72 (= K79), S147 (≠ P161), S148 (≠ G162), S166 (≠ T183), T168 (= T185), G169 (= G186), G170 (= G187), S171 (= S188), Q174 (= Q191)
- binding glutamine: M122 (= M129), G123 (= G130), D167 (= D184), T168 (= T185), G169 (= G186), G170 (= G187), S171 (= S188), F199 (= F216), Y302 (= Y319), R351 (= R367), D418 (= D434)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
48% identity, 98% coverage: 4:492/500 of query aligns to 2:476/478 of 3h0lA
- active site: K72 (= K79), S147 (≠ P161), S148 (≠ G162), S166 (≠ T183), T168 (= T185), G169 (= G186), G170 (= G187), S171 (= S188), Q174 (= Q191)
- binding asparagine: G123 (= G130), S147 (≠ P161), G169 (= G186), G170 (= G187), S171 (= S188), Y302 (= Y319), R351 (= R367), D418 (= D434)
3kfuE Crystal structure of the transamidosome (see paper)
46% identity, 96% coverage: 11:492/500 of query aligns to 4:465/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
36% identity, 81% coverage: 79:482/500 of query aligns to 38:449/450 of 4n0iA
- active site: K38 (= K79), S116 (= S164), S117 (= S165), T135 (= T183), T137 (= T185), G138 (= G186), G139 (= G187), S140 (= S188), L143 (≠ Q191)
- binding glutamine: G89 (= G130), T137 (= T185), G138 (= G186), S140 (= S188), Y168 (≠ F216), Y271 (= Y319), Y272 (= Y320), R320 (= R367), D404 (= D434)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
32% identity, 84% coverage: 71:492/500 of query aligns to 87:506/508 of 3a1iA
- active site: K95 (= K79), S170 (≠ G152), S171 (≠ Q153), G189 (≠ A180), Q191 (≠ T185), G192 (= G186), G193 (= G187), A194 (≠ S188), I197 (≠ Q191)
- binding benzamide: F145 (≠ M129), S146 (≠ G130), G147 (≠ S131), Q191 (≠ T185), G192 (= G186), G193 (= G187), A194 (≠ S188), W327 (≠ Y319)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
33% identity, 95% coverage: 9:483/500 of query aligns to 8:476/487 of 1m21A
- active site: K81 (= K79), S160 (= S164), S161 (= S165), T179 (= T183), T181 (= T185), D182 (≠ G186), G183 (= G187), S184 (= S188), C187 (≠ Q191)
- binding : A129 (= A128), N130 (≠ M129), F131 (≠ G130), C158 (≠ G162), G159 (= G163), S160 (= S164), S184 (= S188), C187 (≠ Q191), I212 (≠ F216), R318 (≠ Y320), L321 (≠ A323), L365 (≠ V374), F426 (vs. gap)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
29% identity, 96% coverage: 7:484/500 of query aligns to 1:449/457 of 6c6gA
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
30% identity, 98% coverage: 4:494/500 of query aligns to 25:498/507 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 (= K79) mutation to A: Abolishes activity on mandelamide.
- S180 (= S164) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S165) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G186) 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 (= S188) mutation to A: Abolishes activity on mandelamide.
- Q207 (= Q191) 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 (≠ A315) 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 (≠ D381) 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 (≠ T439) 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.
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, 96% coverage: 17:497/500 of query aligns to 139:602/607 of Q7XJJ7
- K205 (= K79) mutation to A: Loss of activity.
- SS 281:282 (= SS 164:165) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 185:188) binding
- S305 (= S188) mutation to A: Loss of activity.
- R307 (= R190) mutation to A: Loss of activity.
- S360 (≠ H243) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
27% identity, 96% coverage: 17:497/500 of query aligns to 139:602/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A128), T258 (≠ S131), S281 (= S164), G302 (≠ T185), G303 (= G186), S305 (= S188), S472 (≠ T372), I532 (≠ A429), M539 (vs. gap)
Sites not aligning to the query:
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
31% identity, 85% coverage: 50:475/500 of query aligns to 62:453/605 of Q936X2
- K91 (= K79) mutation to A: Loss of activity.
- S165 (= S164) mutation to A: Loss of activity.
- S189 (= S188) mutation to A: Loss of activity.
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
27% identity, 95% coverage: 10:486/500 of query aligns to 9:476/490 of 4yjiA
- active site: K79 (= K79), S158 (= S164), S159 (= S165), G179 (≠ T185), G180 (= G186), G181 (= G187), A182 (≠ S188)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L81), G132 (≠ A128), S158 (= S164), G179 (≠ T185), G180 (= G186), A182 (≠ S188)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
24% identity, 97% coverage: 5:491/500 of query aligns to 3:452/457 of 5h6sC
- active site: K77 (= K79), S152 (= S164), S153 (= S165), L173 (≠ T185), G174 (= G186), G175 (= G187), S176 (= S188)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A128), R128 (≠ G130), W129 (≠ S131), S152 (= S164), L173 (≠ T185), G174 (= G186), S176 (= S188), W306 (≠ Y319), F338 (≠ Y352)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
31% identity, 85% coverage: 51:475/500 of query aligns to 39:430/461 of 4gysB
- active site: K72 (= K85), S146 (= S164), S147 (= S165), T165 (= T183), T167 (= T185), A168 (≠ G186), G169 (= G187), S170 (= S188), V173 (≠ Q191)
- binding malonate ion: A120 (= A128), G122 (= G130), S146 (= S164), T167 (= T185), A168 (≠ G186), S170 (= S188), S193 (≠ W211), G194 (= G212), V195 (≠ I213), R200 (≠ S218), Y297 (= Y334), R305 (= R342)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
31% identity, 54% coverage: 2:273/500 of query aligns to 1:259/482 of 3a2qA
- active site: K69 (= K79), S147 (≠ P161), S148 (≠ G162), N166 (≠ T183), A168 (≠ T185), A169 (≠ G186), G170 (= G187), A171 (≠ S188), I174 (≠ Q191)
- binding 6-aminohexanoic acid: G121 (≠ A128), G121 (≠ A128), N122 (≠ M129), S147 (≠ P161), A168 (≠ T185), A168 (≠ T185), A169 (≠ G186), A171 (≠ S188)
Sites not aligning to the query:
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
25% identity, 96% coverage: 7:485/500 of query aligns to 2:409/412 of 1o9oA
- active site: K62 (= K79), A131 (≠ R147), S132 (≠ A148), T150 (= T183), T152 (= T185), G153 (= G186), G154 (= G187), S155 (= S188), R158 (≠ Q191)
- binding 3-amino-3-oxopropanoic acid: G130 (≠ R146), T152 (= T185), G153 (= G186), G154 (= G187), S155 (= S188), R158 (≠ Q191), P359 (= P427)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
25% identity, 96% coverage: 7:485/500 of query aligns to 2:409/412 of 1ocmA
- active site: K62 (= K79), S131 (≠ P161), S132 (≠ G162), T152 (= T185), G153 (= G186), G154 (= G187), S155 (= S188)
- binding pyrophosphate 2-: R113 (≠ S132), S131 (≠ P161), Q151 (≠ D184), T152 (= T185), G153 (= G186), G154 (= G187), S155 (= S188), R158 (≠ Q191), P359 (= P427)
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
27% identity, 62% coverage: 3:310/500 of query aligns to 1:341/564 of 6te4A
Sites not aligning to the query:
Query Sequence
>WP_068460249.1 NCBI__GCF_001541235.1:WP_068460249.1
MTDLTKLTIAEARDKLRKKEVSATELTQAFIDAIEVANPQLNAYVRTTPELALKQAEESD
RRLKSGDARPLEGLPLGNKDLFCTKDVETTACSKILEGFTPTYESTVGSNLWNAGAVMLG
KLNCDEFAMGSSNETSAYGPVVSPWRRAGADGQLTSENLVPGGSSGGSSAAVAADLCLGA
TATDTGGSIRQPAALTGTVGIKPTYGRCSRWGIVAFASSLDQAGPLAKTVRDAAIMLRSM
ASHDPKDSTSVETPVPDYELALAQGVKGLRVGVPKEYRVEGMSPDIERLWQEGIEWLKAA
GATIHEVSLPHTKFALPTYYVVAPAEASSNLARYDGVRYGLRVEGKDLIDMYENSRAAGF
GKEVQRRVLIGTYVLSAGYYDAYYLKAQKVRTLIKRDFDDAWQSVDVLLTPTTPTPAFKI
GEKLDDPMAMYAQDIFTVTVNMAGLPGISVPAGISVDGLPLGLQLIGKPFDEATLFRAAQ
VIEDAAGHFKVPQRWWETAR
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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