SitesBLAST
Comparing WP_009543840.1 NCBI__GCF_000017845.1:WP_009543840.1 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)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
30% identity, 96% coverage: 4:454/469 of query aligns to 1:468/482 of 3a2qA
- active site: K69 (= K85), S147 (= S160), S148 (= S161), N166 (≠ S179), A168 (≠ G181), A169 (≠ G182), G170 (= G183), A171 (≠ S184), I174 (≠ G187)
- binding 6-aminohexanoic acid: G121 (= G134), G121 (= G134), N122 (≠ S135), S147 (= S160), A168 (≠ G181), A168 (≠ G181), A169 (≠ G182), A171 (≠ S184), C313 (≠ W319)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
31% identity, 97% coverage: 6:459/469 of query aligns to 3:478/485 of 2f2aA
- active site: K79 (= K85), S154 (= S160), S155 (= S161), S173 (= S179), T175 (≠ G181), G176 (= G182), G177 (= G183), S178 (= S184), Q181 (≠ G187)
- binding glutamine: G130 (≠ F136), S154 (= S160), D174 (= D180), T175 (≠ G181), G176 (= G182), S178 (= S184), F206 (≠ Y212), Y309 (≠ F315), Y310 (≠ T316), R358 (≠ E344), D425 (≠ W404)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
31% identity, 97% coverage: 6:459/469 of query aligns to 3:478/485 of 2dqnA
- active site: K79 (= K85), S154 (= S160), S155 (= S161), S173 (= S179), T175 (≠ G181), G176 (= G182), G177 (= G183), S178 (= S184), Q181 (≠ G187)
- binding asparagine: M129 (≠ S135), G130 (≠ F136), T175 (≠ G181), G176 (= G182), S178 (= S184), Y309 (≠ F315), Y310 (≠ T316), R358 (≠ E344), D425 (≠ W404)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 96% coverage: 13:464/469 of query aligns to 9:476/478 of 3h0mA
- active site: K72 (= K85), S147 (= S160), S148 (= S161), S166 (= S179), T168 (≠ G181), G169 (= G182), G170 (= G183), S171 (= S184), Q174 (≠ G187)
- binding glutamine: M122 (≠ S135), G123 (≠ F136), D167 (= D180), T168 (≠ G181), G169 (= G182), G170 (= G183), S171 (= S184), F199 (≠ Y212), Y302 (≠ F315), R351 (≠ S334), D418 (≠ W404)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 96% coverage: 13:464/469 of query aligns to 9:476/478 of 3h0lA
- active site: K72 (= K85), S147 (= S160), S148 (= S161), S166 (= S179), T168 (≠ G181), G169 (= G182), G170 (= G183), S171 (= S184), Q174 (≠ G187)
- binding asparagine: G123 (≠ F136), S147 (= S160), G169 (= G182), G170 (= G183), S171 (= S184), Y302 (≠ F315), R351 (≠ S334), D418 (≠ W404)
3kfuE Crystal structure of the transamidosome (see paper)
31% identity, 93% coverage: 23:457/469 of query aligns to 14:457/468 of 3kfuE
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
28% identity, 95% coverage: 11:455/469 of query aligns to 7:445/457 of 5h6sC
- active site: K77 (= K85), S152 (= S160), S153 (= S161), L173 (≠ G181), G174 (= G182), G175 (= G183), S176 (= S184)
- binding 4-oxidanylbenzohydrazide: C126 (≠ S135), R128 (≠ P137), W129 (≠ F138), S152 (= S160), L173 (≠ G181), G174 (= G182), S176 (= S184), W306 (≠ F315), F338 (= F340)
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
26% identity, 94% coverage: 13:455/469 of query aligns to 133:589/607 of Q7XJJ7
- K205 (= K85) mutation to A: Loss of activity.
- SS 281:282 (= SS 160:161) mutation to AA: Loss of activity.
- GGGS 302:305 (= GGGS 181:184) binding
- S305 (= S184) mutation to A: Loss of activity.
- R307 (= R186) mutation to A: Loss of activity.
- S360 (≠ Y239) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
26% identity, 94% coverage: 13:455/469 of query aligns to 133:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (= G134), T258 (≠ P137), S281 (= S160), G302 (= G181), G303 (= G182), S305 (= S184), S472 (vs. gap), I532 (vs. gap), M539 (≠ I405)
Sites not aligning to the query:
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
28% identity, 95% coverage: 11:457/469 of query aligns to 8:476/490 of 4yjiA
- active site: K79 (= K85), S158 (= S160), S159 (= S161), G179 (= G181), G180 (= G182), G181 (= G183), A182 (≠ S184)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L87), G132 (= G134), S158 (= S160), G179 (= G181), G180 (= G182), A182 (≠ S184)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
34% identity, 54% coverage: 13:263/469 of query aligns to 7:263/487 of 1m21A
- active site: K81 (= K85), S160 (= S160), S161 (= S161), T179 (≠ S179), T181 (≠ G181), D182 (≠ G182), G183 (= G183), S184 (= S184), C187 (≠ G187)
- binding : A129 (≠ G134), N130 (≠ S135), F131 (= F136), C158 (≠ G158), G159 (= G159), S160 (= S160), S184 (= S184), C187 (≠ G187), I212 (≠ Y212)
Sites not aligning to the query:
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
28% identity, 80% coverage: 79:455/469 of query aligns to 89:498/508 of 3a1iA
- active site: K95 (= K85), S170 (= S160), S171 (= S161), G189 (≠ S179), Q191 (≠ G181), G192 (= G182), G193 (= G183), A194 (≠ S184), I197 (≠ G187)
- binding benzamide: F145 (≠ S135), S146 (≠ F136), G147 (≠ P137), Q191 (≠ G181), G192 (= G182), G193 (= G183), A194 (≠ S184), W327 (vs. gap)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
26% identity, 93% coverage: 17:454/469 of query aligns to 36:487/507 of Q84DC4
- K100 (= K85) mutation to A: Abolishes activity on mandelamide.
- S180 (= S160) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S161) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G182) 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 (= S184) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ G187) 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 (= S296) 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 (≠ R352) 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 (= I405) 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.
Sites not aligning to the query:
- 31 T→I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
28% identity, 91% coverage: 28:456/469 of query aligns to 22:444/461 of 4gysB
- active site: K72 (= K85), S146 (= S160), S147 (= S161), T165 (≠ S179), T167 (≠ G181), A168 (≠ G182), G169 (= G183), S170 (= S184), V173 (≠ G187)
- binding malonate ion: A120 (≠ G134), G122 (≠ F136), S146 (= S160), T167 (≠ G181), A168 (≠ G182), S170 (= S184), S193 (≠ A207), G194 (≠ P208), V195 (= V209), R200 (≠ S214), Y297 (≠ W319), R305 (≠ G327)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
26% identity, 87% coverage: 56:464/469 of query aligns to 72:476/605 of Q936X2
- K91 (= K85) mutation to A: Loss of activity.
- S165 (= S160) mutation to A: Loss of activity.
- S189 (= S184) mutation to A: Loss of activity.
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
26% identity, 85% coverage: 55:454/469 of query aligns to 43:448/457 of 6c6gA
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)
26% identity, 64% coverage: 1:301/469 of query aligns to 69:360/579 of Q9TUI8
- S217 (= S160) mutation to A: Loss of activity.
- S218 (= S161) mutation to A: Lowers activity by at least 98%.
- D237 (= D180) mutation D->E,N: Loss of activity.
- S241 (= S184) mutation to A: Loss of activity.
- C249 (= C192) mutation to A: Loss of activity.
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
34% identity, 41% coverage: 49:238/469 of query aligns to 22:209/412 of 1o9oA
- active site: K62 (= K85), A131 (≠ S160), S132 (= S161), T150 (≠ S179), T152 (≠ G181), G153 (= G182), G154 (= G183), S155 (= S184), R158 (≠ G187)
- binding 3-amino-3-oxopropanoic acid: G130 (= G159), T152 (≠ G181), G153 (= G182), G154 (= G183), S155 (= S184), R158 (≠ G187)
Sites not aligning to the query:
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
35% identity, 41% coverage: 49:238/469 of query aligns to 22:209/412 of 1ocmA
- active site: K62 (= K85), S131 (= S160), S132 (= S161), T152 (≠ G181), G153 (= G182), G154 (= G183), S155 (= S184)
- binding pyrophosphate 2-: R113 (≠ T139), S131 (= S160), Q151 (≠ D180), T152 (≠ G181), G153 (= G182), G154 (= G183), S155 (= S184), R158 (≠ G187)
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)
27% identity, 61% coverage: 16:301/469 of query aligns to 84:360/579 of P97612
- K142 (= K85) mutation to A: Lowers activity 40000-fold. Lowers activity 70000-fold; when associated with A-217.
- S217 (= S160) mutation to A: Lowers activity 3000-fold. Lowers activity 70000-fold; when associated with A-142.
Query Sequence
>WP_009543840.1 NCBI__GCF_000017845.1:WP_009543840.1
MNSVDLAFTPALDLAQLISDRTISPLELTQLYLERIERYNPQLGSFFFIAAETAIQEAKE
KTEQLIHSSNSNGLPPFFGVPTAIKDLNAVAKMPISYGVAALKENIASYDDGVTLRMKEA
GFIILGKTATSQLGSFPFTEPPGFPPARNPWHLDYTPGGSSGGSAAAVAAGLCAIAQGSD
GGGSVRGPAACCGLVGIKPARGRVSHAPVGDYQSGISTNGPLARTVADAAALLDVMSGYI
TGDPYWLPSPDISFSEATKQMSPPLKIAFCDHIPPFTHSETIVKETIQKTVHLLESFGHS
LEMKCPSVETLIEPFTLIWQSAISASGLPSTVLSPLNGWFKEQEITAGEYLRAVHQLQIG
SRHLVAFFDNYDVLLLPVYLHQPIKVGQWKDLSPQETLEKIINWIAPCPAFNASGLPAIT
LPMAQDEKGLPIGIQLVGKPADELTLIRLAAQLEKGNNLSLSIPSSVKD
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