SitesBLAST
Comparing H281DRAFT_06113 FitnessBrowser__Burk376:H281DRAFT_06113 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)
Q9FR37 Amidase 1; AtAMI1; Translocon at the outer membrane of chloroplasts 64-I; AtTOC64-I; EC 3.5.1.4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
31% identity, 82% coverage: 71:447/458 of query aligns to 28:417/425 of Q9FR37
- K36 (= K79) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S162) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S163) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D182) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S186) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (≠ N194) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (≠ A266) mutation to T: Slightly reduces catalytic activity.
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
35% identity, 55% coverage: 42:294/458 of query aligns to 63:307/507 of Q84DC4
- K100 (= K79) mutation to A: Abolishes activity on mandelamide.
- S180 (= S162) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S163) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ A184) 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 (= S186) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ I189) 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.
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.
- 316 S→N: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with H-207 and N-437.
- 382 Q→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.
- 437 I→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)
25% identity, 88% coverage: 50:453/458 of query aligns to 176:589/607 of Q7XJJ7
- K205 (= K79) mutation to A: Loss of activity.
- SS 281:282 (= SS 162:163) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TAGS 183:186) binding
- S305 (= S186) mutation to A: Loss of activity.
- R307 (= R188) mutation to A: Loss of activity.
- S360 (≠ R241) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
25% identity, 88% coverage: 50:453/458 of query aligns to 176:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A129), T258 (≠ G132), S281 (= S162), G302 (≠ T183), G303 (≠ A184), S305 (= S186), S472 (≠ R338), I532 (≠ A400), M539 (≠ L403)
Sites not aligning to the query:
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
41% identity, 38% coverage: 71:242/458 of query aligns to 73:240/487 of 1m21A
- active site: K81 (= K79), S160 (= S162), S161 (= S163), T179 (= T181), T181 (= T183), D182 (≠ A184), G183 (= G185), S184 (= S186), C187 (≠ I189)
- binding : A129 (= A129), N130 (vs. gap), F131 (≠ Y130), C158 (≠ G160), G159 (= G161), S160 (= S162), S184 (= S186), C187 (≠ I189), I212 (≠ L214)
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)
40% identity, 47% coverage: 42:256/458 of query aligns to 37:245/457 of 6c6gA
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
30% identity, 87% coverage: 57:456/458 of query aligns to 69:466/605 of Q936X2
- K91 (= K79) mutation to A: Loss of activity.
- S165 (= S162) mutation to A: Loss of activity.
- S189 (= S186) mutation to A: Loss of activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
32% identity, 93% coverage: 25:448/458 of query aligns to 18:434/461 of 4gysB
- active site: K72 (= K79), S146 (= S162), S147 (= S163), T165 (= T181), T167 (= T183), A168 (= A184), G169 (= G185), S170 (= S186), V173 (≠ I189)
- binding malonate ion: A120 (= A129), G122 (≠ S131), S146 (= S162), T167 (= T183), A168 (= A184), S170 (= S186), S193 (≠ Q209), G194 (= G210), V195 (≠ M211), R200 (≠ K216), Y297 (≠ A305), R305 (≠ A315)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
24% identity, 95% coverage: 23:457/458 of query aligns to 23:478/485 of 2f2aA
- active site: K79 (= K79), S154 (= S162), S155 (= S163), S173 (≠ T181), T175 (= T183), G176 (≠ A184), G177 (= G185), S178 (= S186), Q181 (≠ I189)
- binding glutamine: G130 (= G134), S154 (= S162), D174 (= D182), T175 (= T183), G176 (≠ A184), S178 (= S186), F206 (≠ L214), Y309 (≠ C301), Y310 (≠ D302), R358 (= R338), D425 (≠ N399)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
24% identity, 95% coverage: 23:457/458 of query aligns to 23:478/485 of 2dqnA
- active site: K79 (= K79), S154 (= S162), S155 (= S163), S173 (≠ T181), T175 (= T183), G176 (≠ A184), G177 (= G185), S178 (= S186), Q181 (≠ I189)
- binding asparagine: M129 (≠ L133), G130 (= G134), T175 (= T183), G176 (≠ A184), S178 (= S186), Y309 (≠ C301), Y310 (≠ D302), R358 (= R338), D425 (≠ N399)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
25% identity, 97% coverage: 8:453/458 of query aligns to 4:467/478 of 3h0mA
- active site: K72 (= K79), S147 (= S162), S148 (= S163), S166 (≠ T181), T168 (= T183), G169 (≠ A184), G170 (= G185), S171 (= S186), Q174 (≠ I189)
- binding glutamine: M122 (≠ Y130), G123 (≠ S131), D167 (= D182), T168 (= T183), G169 (≠ A184), G170 (= G185), S171 (= S186), F199 (≠ L214), Y302 (≠ C301), R351 (≠ D344), D418 (≠ N399)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
25% identity, 97% coverage: 8:453/458 of query aligns to 4:467/478 of 3h0lA
- active site: K72 (= K79), S147 (= S162), S148 (= S163), S166 (≠ T181), T168 (= T183), G169 (≠ A184), G170 (= G185), S171 (= S186), Q174 (≠ I189)
- binding asparagine: G123 (≠ S131), S147 (= S162), G169 (≠ A184), G170 (= G185), S171 (= S186), Y302 (≠ C301), R351 (≠ D344), D418 (≠ N399)
Q9MUK5 Translocon at the outer membrane of chloroplasts 64 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
44% identity, 33% coverage: 76:226/458 of query aligns to 66:210/593 of Q9MUK5
Sites not aligning to the query:
- 516 N→A: Loss of HSP90 binding, but no effect on HSP70 binding.
- 550 R→A: 80% decrease of HSP70 and HSP90 binding.
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
33% identity, 46% coverage: 20:231/458 of query aligns to 16:227/457 of 5h6sC
- active site: K77 (= K79), S152 (= S162), S153 (= S163), L173 (≠ T183), G174 (≠ A184), G175 (= G185), S176 (= S186)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A129), R128 (≠ S131), W129 (≠ G132), S152 (= S162), L173 (≠ T183), G174 (≠ A184), S176 (= S186)
Sites not aligning to the query:
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
27% identity, 84% coverage: 71:453/458 of query aligns to 87:498/508 of 3a1iA
- active site: K95 (= K79), S170 (= S162), S171 (= S163), G189 (≠ T181), Q191 (≠ T183), G192 (≠ A184), G193 (= G185), A194 (≠ S186), I197 (= I189)
- binding benzamide: F145 (≠ Y130), S146 (= S131), G147 (= G132), Q191 (≠ T183), G192 (≠ A184), G193 (= G185), A194 (≠ S186), W327 (≠ C301)
3kfuE Crystal structure of the transamidosome (see paper)
41% identity, 42% coverage: 42:232/458 of query aligns to 36:210/468 of 3kfuE
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)
29% identity, 63% coverage: 18:305/458 of query aligns to 4:322/490 of 4yjiA
- active site: K79 (= K79), S158 (= S162), S159 (= S163), G179 (≠ T183), G180 (≠ A184), G181 (= G185), A182 (≠ S186)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L81), G132 (≠ A129), S158 (= S162), G179 (≠ T183), G180 (≠ A184), A182 (≠ S186)
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
33% identity, 48% coverage: 46:264/458 of query aligns to 49:263/564 of 6te4A
Sites not aligning to the query:
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
35% identity, 35% coverage: 67:228/458 of query aligns to 26:182/450 of 4n0iA
- active site: K38 (= K79), S116 (= S162), S117 (= S163), T135 (= T181), T137 (= T183), G138 (≠ A184), G139 (= G185), S140 (= S186), L143 (≠ I189)
- binding glutamine: G89 (≠ S131), T137 (= T183), G138 (≠ A184), S140 (= S186), Y168 (≠ L214)
Sites not aligning to the query:
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
27% identity, 84% coverage: 71:456/458 of query aligns to 54:411/412 of 1o9oA
- active site: K62 (= K79), A131 (≠ S162), S132 (= S163), T150 (= T181), T152 (= T183), G153 (≠ A184), G154 (= G185), S155 (= S186), R158 (≠ I189)
- binding 3-amino-3-oxopropanoic acid: G130 (= G161), T152 (= T183), G153 (≠ A184), G154 (= G185), S155 (= S186), R158 (≠ I189), P359 (= P393)
Query Sequence
>H281DRAFT_06113 FitnessBrowser__Burk376:H281DRAFT_06113
LNVPSWDQRSAVGLAHSYGEGSADVEGVVREAIDRARACNAAFIDVTEARALEESRAAAA
RWREKRPASALDGVPIAWKDLFDVAGTVSTAGSALFRGRPPATADAPLVAAGARAGFVCI
GKTNLSEFAYSGLGLNPHFGTPFNSAFDATVEGGGHRVPGGSSSGAAIAVAAGVVPIAVG
TDTAGSIRIPAALNGVVGYRASSARYPQQGMIGLSKSADTCGPLARSVADCAAFDAVVRG
RELPRSLAGLRGQPFVVPLGWESRFAVTNDVGDNFMRFVARLSKAGARIQQVRVRAFDAA
CDLIATRGWFGSLEAFEAYRSVLDSDDAKRIDQRVRTRLELSRDVPASRLAELLAERGRL
LGEFGAEIDGATLLLPTVPHVAPECAPLEADPPRFAAVNAATLSMTMPGSFLDTPAFAMP
TGADPAGLPTSVQLMRAQNDDDALIALALAVEQTVALD
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