SitesBLAST
Comparing WP_013529596.1 NCBI__GCF_000185905.1:WP_013529596.1 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)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
31% identity, 95% coverage: 20:479/483 of query aligns to 7:478/490 of 4yjiA
- active site: K79 (= K93), S158 (= S168), S159 (= S169), G179 (≠ F189), G180 (= G190), G181 (= G191), A182 (≠ S192)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L95), G132 (= G142), S158 (= S168), G179 (≠ F189), G180 (= G190), A182 (≠ S192)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
31% identity, 96% coverage: 15:478/483 of query aligns to 1:448/457 of 5h6sC
- active site: K77 (= K93), S152 (= S168), S153 (= S169), L173 (≠ F189), G174 (= G190), G175 (= G191), S176 (= S192)
- binding 4-oxidanylbenzohydrazide: C126 (≠ G142), R128 (≠ G144), W129 (≠ S145), S152 (= S168), L173 (≠ F189), G174 (= G190), S176 (= S192), W306 (= W322), F338 (vs. gap)
3kfuE Crystal structure of the transamidosome (see paper)
35% identity, 93% coverage: 24:474/483 of query aligns to 1:454/468 of 3kfuE
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
27% identity, 94% coverage: 20:475/483 of query aligns to 7:474/485 of 2f2aA
- active site: K79 (= K93), S154 (= S168), S155 (= S169), S173 (= S187), T175 (≠ F189), G176 (= G190), G177 (= G191), S178 (= S192), Q181 (≠ N195)
- binding glutamine: G130 (= G144), S154 (= S168), D174 (= D188), T175 (≠ F189), G176 (= G190), S178 (= S192), F206 (= F221), Y309 (≠ Q323), Y310 (≠ A324), R358 (≠ Q368), D425 (≠ M425)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
27% identity, 94% coverage: 20:475/483 of query aligns to 7:474/485 of 2dqnA
- active site: K79 (= K93), S154 (= S168), S155 (= S169), S173 (= S187), T175 (≠ F189), G176 (= G190), G177 (= G191), S178 (= S192), Q181 (≠ N195)
- binding asparagine: M129 (≠ L143), G130 (= G144), T175 (≠ F189), G176 (= G190), S178 (= S192), Y309 (≠ Q323), Y310 (≠ A324), R358 (≠ Q368), D425 (≠ M425)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 96% coverage: 16:477/483 of query aligns to 2:469/478 of 3h0mA
- active site: K72 (= K93), S147 (= S168), S148 (= S169), S166 (= S187), T168 (≠ F189), G169 (= G190), G170 (= G191), S171 (= S192), Q174 (≠ N195)
- binding glutamine: M122 (≠ L143), G123 (= G144), D167 (= D188), T168 (≠ F189), G169 (= G190), G170 (= G191), S171 (= S192), F199 (= F221), Y302 (≠ Q323), R351 (vs. gap), D418 (= D419)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 96% coverage: 16:477/483 of query aligns to 2:469/478 of 3h0lA
- active site: K72 (= K93), S147 (= S168), S148 (= S169), S166 (= S187), T168 (≠ F189), G169 (= G190), G170 (= G191), S171 (= S192), Q174 (≠ N195)
- binding asparagine: G123 (= G144), S147 (= S168), G169 (= G190), G170 (= G191), S171 (= S192), Y302 (≠ Q323), R351 (vs. gap), D418 (= D419)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
27% identity, 95% coverage: 18:477/483 of query aligns to 27:490/507 of Q84DC4
- T31 (≠ V22) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K93) mutation to A: Abolishes activity on mandelamide.
- S180 (= S168) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S169) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G190) 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 (= S192) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ N195) 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 (vs. gap) 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 (≠ A366) 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 (≠ M425) 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.
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
29% identity, 95% coverage: 19:476/483 of query aligns to 1:450/457 of 6c6gA
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
34% identity, 51% coverage: 14:260/483 of query aligns to 6:251/487 of 1m21A
- active site: K81 (= K93), S160 (= S168), S161 (= S169), T179 (≠ S187), T181 (≠ F189), D182 (≠ G190), G183 (= G191), S184 (= S192), C187 (≠ N195)
- binding : A129 (≠ G142), N130 (vs. gap), F131 (vs. gap), C158 (≠ G166), G159 (= G167), S160 (= S168), S184 (= S192), C187 (≠ N195), I212 (≠ V220)
Sites not aligning to the query:
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
34% identity, 49% coverage: 15:250/483 of query aligns to 1:241/564 of 6te4A
Sites not aligning to the query:
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
28% identity, 88% coverage: 34:458/483 of query aligns to 17:422/461 of 4gysB
- active site: K72 (= K93), S146 (= S168), S147 (= S169), T165 (≠ S187), T167 (≠ F189), A168 (≠ G190), G169 (= G191), S170 (= S192), V173 (≠ N195)
- binding malonate ion: A120 (≠ G142), G122 (= G144), S146 (= S168), T167 (≠ F189), A168 (≠ G190), S170 (= S192), S193 (≠ G215), G194 (≠ E219), V195 (= V220), R200 (≠ M225), Y297 (vs. gap), R305 (= R329)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
35% identity, 48% coverage: 21:250/483 of query aligns to 7:231/482 of 3a2qA
- active site: K69 (= K93), S147 (= S168), S148 (= S169), N166 (≠ S187), A168 (≠ F189), A169 (≠ G190), G170 (= G191), A171 (≠ S192), I174 (≠ N195)
- binding 6-aminohexanoic acid: G121 (= G142), G121 (= G142), N122 (≠ L143), S147 (= S168), A168 (≠ F189), A168 (≠ F189), A169 (≠ G190), A171 (≠ S192)
Sites not aligning to the query:
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
27% identity, 90% coverage: 37:473/483 of query aligns to 37:460/605 of Q936X2
- K91 (= K93) mutation to A: Loss of activity.
- S165 (= S168) mutation to A: Loss of activity.
- S189 (= S192) mutation to A: Loss of activity.
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
28% identity, 83% coverage: 83:481/483 of query aligns to 85:507/508 of 3a1iA
- active site: K95 (= K93), S170 (= S168), S171 (= S169), G189 (≠ S187), Q191 (≠ F189), G192 (= G190), G193 (= G191), A194 (≠ S192), I197 (≠ N195)
- binding benzamide: F145 (≠ L143), S146 (≠ G144), G147 (≠ S145), Q191 (≠ F189), G192 (= G190), G193 (= G191), A194 (≠ S192), W327 (= W322)
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
41% identity, 26% coverage: 85:210/483 of query aligns to 30:158/450 of 4n0iA
- active site: K38 (= K93), S116 (= S168), S117 (= S169), T135 (≠ S187), T137 (≠ F189), G138 (= G190), G139 (= G191), S140 (= S192), L143 (≠ N195)
- binding glutamine: G89 (= G144), T137 (≠ F189), G138 (= G190), S140 (= S192)
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, 44% coverage: 23:235/483 of query aligns to 81:287/579 of Q9TUI8
- S217 (= S168) mutation to A: Loss of activity.
- S218 (= S169) mutation to A: Lowers activity by at least 98%.
- D237 (= D188) mutation D->E,N: Loss of activity.
- S241 (= S192) mutation to A: Loss of activity.
- C249 (≠ N200) mutation to A: Loss of activity.
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
32% identity, 40% coverage: 19:213/483 of query aligns to 2:176/412 of 1o9oA
- active site: K62 (= K93), A131 (≠ S168), S132 (= S169), T150 (≠ S187), T152 (≠ F189), G153 (= G190), G154 (= G191), S155 (= S192), R158 (≠ N195)
- binding 3-amino-3-oxopropanoic acid: G130 (= G167), T152 (≠ F189), G153 (= G190), G154 (= G191), S155 (= S192), R158 (≠ N195)
Sites not aligning to the query:
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
33% identity, 40% coverage: 19:213/483 of query aligns to 2:176/412 of 1ocmA
- active site: K62 (= K93), S131 (= S168), S132 (= S169), T152 (≠ F189), G153 (= G190), G154 (= G191), S155 (= S192)
- binding pyrophosphate 2-: R113 (≠ G144), S131 (= S168), Q151 (≠ D188), T152 (≠ F189), G153 (= G190), G154 (= G191), S155 (= S192), R158 (≠ N195)
Sites not aligning to the query:
P97612 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 Rattus norvegicus (Rat) (see paper)
28% identity, 43% coverage: 28:235/483 of query aligns to 86:287/579 of P97612
- K142 (= K93) mutation to A: Lowers activity 40000-fold. Lowers activity 70000-fold; when associated with A-217.
- S217 (= S168) mutation to A: Lowers activity 3000-fold. Lowers activity 70000-fold; when associated with A-142.
Query Sequence
>WP_013529596.1 NCBI__GCF_000185905.1:WP_013529596.1
MLRPHTKHAVPPASDICRLSAVQLAGAIRGRELSVREVVAAFLDRIEAVNPLVNAIVSLR
DRADILREADAADASLSRTEAAGPLFGLPMAIKDLASTTGLRTSFGSPIFADFVPQEDDF
FVERIRNAGAIIIGKTNVPEFGLGSNTYNAVFGPTLNAFDPALTAGGSSGGAAVALALDM
VPVADGSDFGGSLRNPAAWNNVFGFRPSQGLVPGGPDFEVFHAQMGVDGPMGRNVGDMAL
LLDVQAGYHPHAPLSYEKPGSFLEGLGIPATGGRIAWLGDLGGHLPVETGILGLCEAALG
RFAEASFATEPLLPDFDFEALWQAFVTLRQASSGCALKTHYDDPAKRRLLKPEAIWEVEN
ATRLTAPQIRAASVIRTSWHRTLLSIFDRYDLIALPTAQVFPFDIDTHWPREVAGRTMDS
YHRWMQVSAFATLGGCPAANVPVGFDDRGRPMGMQLIGRPRGDLAVLKAAAAYEATLPWP
AGA
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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