SitesBLAST
Comparing H281DRAFT_05429 FitnessBrowser__Burk376:H281DRAFT_05429 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)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
44% identity, 96% coverage: 10:423/432 of query aligns to 2:411/412 of 1o9oA
- active site: K62 (= K75), A131 (≠ S144), S132 (= S145), T150 (≠ S163), T152 (= T165), G153 (= G166), G154 (= G167), S155 (= S168), R158 (= R171)
- binding 3-amino-3-oxopropanoic acid: G130 (= G143), T152 (= T165), G153 (= G166), G154 (= G167), S155 (= S168), R158 (= R171), P359 (= P370)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
44% identity, 96% coverage: 10:423/432 of query aligns to 2:411/412 of 1ocmA
- active site: K62 (= K75), S131 (= S144), S132 (= S145), T152 (= T165), G153 (= G166), G154 (= G167), S155 (= S168)
- binding pyrophosphate 2-: R113 (≠ M126), S131 (= S144), Q151 (= Q164), T152 (= T165), G153 (= G166), G154 (= G167), S155 (= S168), R158 (= R171), P359 (= P370)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
29% identity, 88% coverage: 37:417/432 of query aligns to 33:470/485 of 2f2aA
- active site: K79 (= K75), S154 (= S144), S155 (= S145), S173 (= S163), T175 (= T165), G176 (= G166), G177 (= G167), S178 (= S168), Q181 (≠ R171)
- binding glutamine: G130 (≠ M126), S154 (= S144), D174 (≠ Q164), T175 (= T165), G176 (= G166), S178 (= S168), F206 (= F196), Y309 (≠ H285), Y310 (≠ E286), R358 (vs. gap), D425 (≠ T377)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
29% identity, 88% coverage: 37:417/432 of query aligns to 33:470/485 of 2dqnA
- active site: K79 (= K75), S154 (= S144), S155 (= S145), S173 (= S163), T175 (= T165), G176 (= G166), G177 (= G167), S178 (= S168), Q181 (≠ R171)
- binding asparagine: M129 (≠ Y125), G130 (≠ M126), T175 (= T165), G176 (= G166), S178 (= S168), Y309 (≠ H285), Y310 (≠ E286), R358 (vs. gap), D425 (≠ T377)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 96% coverage: 14:429/432 of query aligns to 12:476/478 of 3h0mA
- active site: K72 (= K75), S147 (= S144), S148 (= S145), S166 (= S163), T168 (= T165), G169 (= G166), G170 (= G167), S171 (= S168), Q174 (≠ R171)
- binding glutamine: M122 (vs. gap), G123 (vs. gap), D167 (≠ Q164), T168 (= T165), G169 (= G166), G170 (= G167), S171 (= S168), F199 (= F196), Y302 (≠ T279), R351 (≠ A319), D418 (≠ G368)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 96% coverage: 14:429/432 of query aligns to 12:476/478 of 3h0lA
- active site: K72 (= K75), S147 (= S144), S148 (= S145), S166 (= S163), T168 (= T165), G169 (= G166), G170 (= G167), S171 (= S168), Q174 (≠ R171)
- binding asparagine: G123 (vs. gap), S147 (= S144), G169 (= G166), G170 (= G167), S171 (= S168), Y302 (≠ T279), R351 (≠ A319), D418 (≠ G368)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
29% identity, 83% coverage: 66:422/432 of query aligns to 91:490/507 of Q84DC4
- K100 (= K75) mutation to A: Abolishes activity on mandelamide.
- S180 (= S144) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S145) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G166) 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 (= S168) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ R171) 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 (≠ T324) 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 (≠ G365) 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.
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)
47% identity, 35% coverage: 67:219/432 of query aligns to 28:185/425 of Q9FR37
- K36 (= K75) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S144) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S145) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (≠ Q164) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S168) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C176) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 214 S→T: Slightly reduces catalytic activity.
3kfuE Crystal structure of the transamidosome (see paper)
31% identity, 91% coverage: 29:423/432 of query aligns to 19:458/468 of 3kfuE
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
36% identity, 49% coverage: 14:223/432 of query aligns to 10:239/487 of 1m21A
- active site: K81 (= K75), S160 (= S144), S161 (= S145), T179 (≠ S163), T181 (= T165), D182 (≠ G166), G183 (= G167), S184 (= S168), C187 (≠ R171)
- binding : A129 (= A124), N130 (vs. gap), F131 (vs. gap), C158 (≠ G142), G159 (= G143), S160 (= S144), S184 (= S168), C187 (≠ R171), I212 (≠ F196)
Sites not aligning to the query:
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
29% identity, 82% coverage: 67:420/432 of query aligns to 197:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A124), T258 (≠ P128), S281 (= S144), G302 (≠ T165), G303 (= G166), S305 (= S168), S472 (vs. gap), I532 (vs. gap), M539 (≠ P370)
Sites not aligning to the query:
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
29% identity, 82% coverage: 67:420/432 of query aligns to 197:589/607 of Q7XJJ7
- K205 (= K75) mutation to A: Loss of activity.
- SS 281:282 (= SS 144:145) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 165:168) binding
- S305 (= S168) mutation to A: Loss of activity.
- R307 (≠ I170) mutation to A: Loss of activity.
- S360 (= S221) mutation to A: No effect.
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
42% identity, 45% coverage: 29:222/432 of query aligns to 20:228/457 of 6c6gA
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
41% identity, 38% coverage: 62:223/432 of query aligns to 82:249/508 of 3a1iA
- active site: K95 (= K75), S170 (= S144), S171 (= S145), G189 (≠ S163), Q191 (≠ T165), G192 (= G166), G193 (= G167), A194 (≠ S168), I197 (≠ R171)
- binding benzamide: F145 (≠ Y125), S146 (≠ M126), G147 (≠ A127), Q191 (≠ T165), G192 (= G166), G193 (= G167), A194 (≠ S168)
Sites not aligning to the query:
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
31% identity, 83% coverage: 66:423/432 of query aligns to 82:466/605 of Q936X2
- K91 (= K75) mutation to A: Loss of activity.
- S165 (vs. gap) mutation to A: Loss of activity.
- S189 (= S168) mutation to A: Loss of activity.
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
25% identity, 95% coverage: 10:420/432 of query aligns to 5:445/457 of 5h6sC
- active site: K77 (= K75), S152 (= S144), S153 (= S145), L173 (≠ T165), G174 (= G166), G175 (= G167), S176 (= S168)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A124), R128 (vs. gap), W129 (≠ Y125), S152 (= S144), L173 (≠ T165), G174 (= G166), S176 (= S168), W306 (≠ F291), F338 (vs. gap)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
38% identity, 46% coverage: 26:224/432 of query aligns to 21:230/482 of 3a2qA
- active site: K69 (= K75), S147 (= S144), S148 (= S145), N166 (≠ S163), A168 (≠ T165), A169 (≠ G166), G170 (= G167), A171 (≠ S168), I174 (≠ R171)
- binding 6-aminohexanoic acid: G121 (≠ A124), G121 (≠ A124), N122 (≠ Y125), S147 (= S144), A168 (≠ T165), A168 (≠ T165), A169 (≠ G166), A171 (≠ S168)
Sites not aligning to the query:
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
25% identity, 85% coverage: 51:419/432 of query aligns to 14:447/450 of 4n0iA
- active site: K38 (= K75), S116 (= S144), S117 (= S145), T135 (≠ S163), T137 (= T165), G138 (= G166), G139 (= G167), S140 (= S168), L143 (≠ R171)
- binding glutamine: G89 (≠ A127), T137 (= T165), G138 (= G166), S140 (= S168), Y168 (≠ F196), Y271 (≠ H285), Y272 (≠ E286), R320 (= R318), D404 (≠ P370)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
41% identity, 40% coverage: 49:222/432 of query aligns to 40:224/461 of 4gysB
- active site: K72 (= K75), S146 (= S144), S147 (= S145), T165 (≠ S163), T167 (= T165), A168 (≠ G166), G169 (= G167), S170 (= S168), V173 (≠ R171)
- binding malonate ion: A120 (= A124), G122 (≠ A127), S146 (= S144), T167 (= T165), A168 (≠ G166), S170 (= S168), S193 (≠ V191), G194 (= G192), V195 (≠ M193), R200 (≠ W198)
Sites not aligning to the query:
Q9MUK5 Translocon at the outer membrane of chloroplasts 64 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
26% identity, 79% coverage: 68:408/432 of query aligns to 62:440/593 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.
Query Sequence
>H281DRAFT_05429 FitnessBrowser__Burk376:H281DRAFT_05429
MNQTSFYRPVSGLDLLKRIDGDARERGCISEEALGRIDDVDPHVRAMTAIARREAVVAAS
ASASGPLAGLPVAVKDIFDTSDLVTSFGSPIYEGYQPRSDATIVTLLRRNGGTIVGKTVT
SEFAYMAPTGTRNPCDIGRTAGGSSSGSAAAVAAGMVPFAIGSQTGGSTIRPASFCGIAG
YKPTLGLLPTVGMKCFSWSFDTIGLFAAGVRDVAYLAQVLSGRRLAVDVAPASPVFGVPD
GYPWTGASANATTALGTAVRSIERAGGRVRPVRFSTWMTDMIDAHETIQSFEAYQTLGYE
YDHHRAELSAKLSEFLDRASALDTATYVNACALMEQAKVRLSELFEGIDVLLTPSARDEA
PDGLGSTGDPAFNRNWTLLGCPCVNVPGLWGARGGPIGVQVIGRPGEDARSLAAAAFVEQ
AIAASAGRPRLM
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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