SitesBLAST
Comparing Ga0059261_3751 FitnessBrowser__Korea:Ga0059261_3751 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)
30% identity, 89% coverage: 47:507/518 of query aligns to 8:478/490 of 4yjiA
- active site: K79 (= K119), S158 (= S194), S159 (= S195), G179 (≠ F215), G180 (= G216), G181 (= G217), A182 (≠ S218)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ T121), G132 (≠ A168), S158 (= S194), G179 (≠ F215), G180 (= G216), A182 (≠ S218)
3kfuE Crystal structure of the transamidosome (see paper)
35% identity, 88% coverage: 50:505/518 of query aligns to 1:457/468 of 3kfuE
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
30% identity, 89% coverage: 52:513/518 of query aligns to 8:455/457 of 5h6sC
- active site: K77 (= K119), S152 (= S194), S153 (= S195), L173 (≠ F215), G174 (= G216), G175 (= G217), S176 (= S218)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A168), R128 (≠ G170), W129 (≠ S171), S152 (= S194), L173 (≠ F215), G174 (= G216), S176 (= S218), W306 (= W349), F338 (vs. gap)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
26% identity, 88% coverage: 49:502/518 of query aligns to 10:473/485 of 2f2aA
- active site: K79 (= K119), S154 (= S194), S155 (= S195), S173 (= S213), T175 (≠ F215), G176 (= G216), G177 (= G217), S178 (= S218), Q181 (≠ N221)
- binding glutamine: G130 (= G170), S154 (= S194), D174 (= D214), T175 (≠ F215), G176 (= G216), S178 (= S218), F206 (= F247), Y309 (≠ T351), Y310 (≠ A352), R358 (≠ Q395), D425 (≠ E444)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
26% identity, 88% coverage: 49:502/518 of query aligns to 10:473/485 of 2dqnA
- active site: K79 (= K119), S154 (= S194), S155 (= S195), S173 (= S213), T175 (≠ F215), G176 (= G216), G177 (= G217), S178 (= S218), Q181 (≠ N221)
- binding asparagine: M129 (≠ L169), G130 (= G170), T175 (≠ F215), G176 (= G216), S178 (= S218), Y309 (≠ T351), Y310 (≠ A352), R358 (≠ Q395), D425 (≠ E444)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
31% identity, 76% coverage: 109:503/518 of query aligns to 85:498/508 of 3a1iA
- active site: K95 (= K119), S170 (= S194), S171 (= S195), G189 (≠ S213), Q191 (≠ F215), G192 (= G216), G193 (= G217), A194 (≠ S218), I197 (≠ N221)
- binding benzamide: F145 (≠ L169), S146 (≠ G170), G147 (≠ S171), Q191 (≠ F215), G192 (= G216), G193 (= G217), A194 (≠ S218), W327 (= W349)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
29% identity, 87% coverage: 54:503/518 of query aligns to 37:488/507 of Q84DC4
- K100 (= K119) mutation to A: Abolishes activity on mandelamide.
- S180 (= S194) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S195) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G216) 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 (= S218) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ N221) 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 (≠ G393) 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 (≠ M452) 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.
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
25% identity, 88% coverage: 49:503/518 of query aligns to 9:467/478 of 3h0mA
- active site: K72 (= K119), S147 (= S194), S148 (= S195), S166 (= S213), T168 (≠ F215), G169 (= G216), G170 (= G217), S171 (= S218), Q174 (≠ N221)
- binding glutamine: M122 (≠ L169), G123 (= G170), D167 (= D214), T168 (≠ F215), G169 (= G216), G170 (= G217), S171 (= S218), F199 (= F247), Y302 (vs. gap), R351 (≠ Q376), D418 (= D446)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
25% identity, 88% coverage: 49:503/518 of query aligns to 9:467/478 of 3h0lA
- active site: K72 (= K119), S147 (= S194), S148 (= S195), S166 (= S213), T168 (≠ F215), G169 (= G216), G170 (= G217), S171 (= S218), Q174 (≠ N221)
- binding asparagine: G123 (= G170), S147 (= S194), G169 (= G216), G170 (= G217), S171 (= S218), Y302 (vs. gap), R351 (≠ Q376), D418 (= D446)
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, 79% coverage: 100:506/518 of query aligns to 181:592/607 of Q7XJJ7
- K205 (= K119) mutation to A: Loss of activity.
- SS 281:282 (= SS 194:195) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ FGGS 215:218) binding
- S305 (= S218) mutation to A: Loss of activity.
- R307 (= R220) mutation to A: Loss of activity.
- S360 (≠ P274) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
26% identity, 79% coverage: 100:506/518 of query aligns to 181:592/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A168), T258 (≠ S171), S281 (= S194), G302 (≠ F215), G303 (= G216), S305 (= S218), S472 (≠ E384), I532 (= I440), M539 (= M452)
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)
30% identity, 89% coverage: 45:503/518 of query aligns to 1:449/457 of 6c6gA
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
30% identity, 88% coverage: 46:503/518 of query aligns to 7:477/487 of 1m21A
- active site: K81 (= K119), S160 (= S194), S161 (= S195), T179 (≠ S213), T181 (≠ F215), D182 (≠ G216), G183 (= G217), S184 (= S218), C187 (≠ N221)
- binding : A129 (= A168), N130 (vs. gap), F131 (vs. gap), C158 (≠ G192), G159 (= G193), S160 (= S194), S184 (= S218), C187 (≠ N221), I212 (≠ S243), R318 (vs. gap), L321 (≠ R356), L365 (≠ V396), F426 (≠ M445)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
28% identity, 90% coverage: 46:510/518 of query aligns to 6:476/482 of 3a2qA
- active site: K69 (= K119), S147 (= S194), S148 (= S195), N166 (≠ S213), A168 (≠ F215), A169 (≠ G216), G170 (= G217), A171 (≠ S218), I174 (≠ N221)
- binding 6-aminohexanoic acid: G121 (≠ A168), G121 (≠ A168), N122 (≠ L169), S147 (= S194), A168 (≠ F215), A168 (≠ F215), A169 (≠ G216), A171 (≠ S218), C313 (≠ R350)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
28% identity, 79% coverage: 92:501/518 of query aligns to 61:460/605 of Q936X2
- K91 (= K119) mutation to A: Loss of activity.
- S165 (= S194) mutation to A: Loss of activity.
- S189 (= S218) mutation to A: Loss of activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
38% identity, 37% coverage: 89:281/518 of query aligns to 45:232/461 of 4gysB
- active site: K72 (= K119), S146 (= S194), S147 (= S195), T165 (≠ S213), T167 (≠ F215), A168 (≠ G216), G169 (= G217), S170 (= S218), V173 (≠ N221)
- binding malonate ion: A120 (= A168), G122 (= G170), S146 (= S194), T167 (≠ F215), A168 (≠ G216), S170 (= S218), S193 (vs. gap), G194 (vs. gap), V195 (vs. gap), R200 (≠ P242)
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)
30% identity, 46% coverage: 26:262/518 of query aligns to 58:288/579 of Q9TUI8
- S217 (= S194) mutation to A: Loss of activity.
- S218 (= S195) mutation to A: Lowers activity by at least 98%.
- D237 (= D214) mutation D->E,N: Loss of activity.
- S241 (= S218) mutation to A: Loss of activity.
- C249 (≠ N226) mutation to A: Loss of activity.
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
33% identity, 46% coverage: 41:277/518 of query aligns to 1:244/564 of 6te4A
Sites not aligning to the query:
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
28% identity, 73% coverage: 109:485/518 of query aligns to 52:390/412 of 1o9oA
- active site: K62 (= K119), A131 (≠ S194), S132 (= S195), T150 (≠ S213), T152 (≠ F215), G153 (= G216), G154 (= G217), S155 (= S218), R158 (≠ N221)
- binding 3-amino-3-oxopropanoic acid: G130 (= G193), T152 (≠ F215), G153 (= G216), G154 (= G217), S155 (= S218), R158 (≠ N221), P359 (≠ D446)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
28% identity, 73% coverage: 109:485/518 of query aligns to 52:390/412 of 1ocmA
- active site: K62 (= K119), S131 (= S194), S132 (= S195), T152 (≠ F215), G153 (= G216), G154 (= G217), S155 (= S218)
- binding pyrophosphate 2-: R113 (≠ F174), S131 (= S194), Q151 (≠ D214), T152 (≠ F215), G153 (= G216), G154 (= G217), S155 (= S218), R158 (≠ N221), P359 (≠ D446)
Query Sequence
>Ga0059261_3751 FitnessBrowser__Korea:Ga0059261_3751
MRTDPEPNGTPITRRALLAAPAAFAASQALATSRPVVGTNSITAMDAVDLVTAIRRRVLS
AREVMTAHLEQIDTLNPRFNAIVSRVAPERLLKAAAACDADAAAGRFHGPLHGFPHAVKD
TAPAAGIPFTQGTPILRENVPTADSLVVSRMRNAGAIFIGKTNVPEFALGSHSFNPLFGV
TRNAWNPAVSAGGSSGGAAVALALRMVPLADGSDFGGSLRNPAGWNNVFGYRPSFGRVPS
VPSSDVFGQTFAVSGPMARRVRDVAFLLSVQAGPDSRSPFSLTEDPARFAGSLDREWKGR
RVGWLGDLQGALATEPGVLDTCEKALSAFRSIGMAVEAARLSLSAEEMWRTAVTLRHWSV
GADLIGHYSDPAKRRQMKPEAIWEVEGYLKLTGRQVAEASEGRARIYQAFRDLFDRYDFL
ILPTAQVFPFDVEQHWPRSIAGREMDSYHRWMEVTLPATMAGLPVLAAPAGFGGARRLPI
GIQIIGPNHADLAVLQVGHAYENASPWIAQALPGALRR
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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