SitesBLAST
Comparing H281DRAFT_03959 FitnessBrowser__Burk376:H281DRAFT_03959 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)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
33% identity, 95% coverage: 22:455/459 of query aligns to 41:490/507 of Q84DC4
- K100 (= K83) mutation to A: Abolishes activity on mandelamide.
- S180 (= S164) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S165) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G186) 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 (= S188) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ I191) 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 (≠ P303) 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 (≠ D348) 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 (≠ L404) 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.
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
36% identity, 81% coverage: 13:386/459 of query aligns to 5:379/457 of 6c6gA
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
28% identity, 89% coverage: 47:454/459 of query aligns to 169:590/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A133), T258 (≠ G136), S281 (= S164), G302 (≠ T185), G303 (= G186), S305 (= S188), S472 (≠ L335), I532 (≠ G397), M539 (≠ L404)
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)
28% identity, 89% coverage: 47:454/459 of query aligns to 169:590/607 of Q7XJJ7
- K205 (= K83) mutation to A: Loss of activity.
- SS 281:282 (= SS 164:165) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 185:188) binding
- S305 (= S188) mutation to A: Loss of activity.
- R307 (= R190) mutation to A: Loss of activity.
- S360 (vs. gap) mutation to A: No effect.
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
28% identity, 90% coverage: 46:456/459 of query aligns to 42:477/485 of 2f2aA
- active site: K79 (= K83), S154 (= S164), S155 (= S165), S173 (≠ T183), T175 (= T185), G176 (= G186), G177 (= G187), S178 (= S188), Q181 (≠ I191)
- binding glutamine: G130 (≠ S135), S154 (= S164), D174 (= D184), T175 (= T185), G176 (= G186), S178 (= S188), F206 (≠ L216), Y309 (vs. gap), Y310 (vs. gap), R358 (= R337), D425 (≠ A401)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
28% identity, 90% coverage: 46:456/459 of query aligns to 42:477/485 of 2dqnA
- active site: K79 (= K83), S154 (= S164), S155 (= S165), S173 (≠ T183), T175 (= T185), G176 (= G186), G177 (= G187), S178 (= S188), Q181 (≠ I191)
- binding asparagine: M129 (≠ F134), G130 (≠ S135), T175 (= T185), G176 (= G186), S178 (= S188), Y309 (vs. gap), Y310 (vs. gap), R358 (= R337), D425 (≠ A401)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 95% coverage: 11:447/459 of query aligns to 7:461/478 of 3h0mA
- active site: K72 (= K83), S147 (= S164), S148 (= S165), S166 (≠ T183), T168 (= T185), G169 (= G186), G170 (= G187), S171 (= S188), Q174 (≠ I191)
- binding glutamine: M122 (≠ L137), G123 (= G138), D167 (= D184), T168 (= T185), G169 (= G186), G170 (= G187), S171 (= S188), F199 (≠ L216), Y302 (vs. gap), R351 (= R337), D418 (≠ N400)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 95% coverage: 11:447/459 of query aligns to 7:461/478 of 3h0lA
- active site: K72 (= K83), S147 (= S164), S148 (= S165), S166 (≠ T183), T168 (= T185), G169 (= G186), G170 (= G187), S171 (= S188), Q174 (≠ I191)
- binding asparagine: G123 (= G138), S147 (= S164), G169 (= G186), G170 (= G187), S171 (= S188), Y302 (vs. gap), R351 (= R337), D418 (≠ N400)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
30% identity, 96% coverage: 13:452/459 of query aligns to 9:444/457 of 5h6sC
- active site: K77 (= K83), S152 (= S164), S153 (= S165), L173 (≠ T185), G174 (= G186), G175 (= G187), S176 (= S188)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A133), R128 (≠ S135), W129 (≠ G136), S152 (= S164), L173 (≠ T185), G174 (= G186), S176 (= S188), W306 (≠ G309), F338 (≠ K340)
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)
29% identity, 81% coverage: 75:447/459 of query aligns to 28:417/425 of Q9FR37
- K36 (= K83) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S164) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S165) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D184) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S188) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C196) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (≠ G255) mutation to T: Slightly reduces catalytic activity.
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
32% identity, 85% coverage: 59:449/459 of query aligns to 69:458/605 of Q936X2
- K91 (= K83) mutation to A: Loss of activity.
- S165 (= S164) mutation to A: Loss of activity.
- S189 (= S188) mutation to A: Loss of activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
32% identity, 95% coverage: 11:447/459 of query aligns to 5:433/461 of 4gysB
- active site: K72 (= K83), S146 (= S164), S147 (= S165), T165 (= T183), T167 (= T185), A168 (≠ G186), G169 (= G187), S170 (= S188), V173 (≠ I191)
- binding malonate ion: A120 (= A133), G122 (≠ S135), S146 (= S164), T167 (= T185), A168 (≠ G186), S170 (= S188), S193 (≠ Q211), G194 (= G212), V195 (≠ G213), R200 (≠ P218), Y297 (≠ R307), R305 (≠ P312)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
30% identity, 84% coverage: 75:458/459 of query aligns to 87:503/508 of 3a1iA
- active site: K95 (= K83), S170 (= S164), S171 (= S165), G189 (≠ T183), Q191 (≠ T185), G192 (= G186), G193 (= G187), A194 (≠ S188), I197 (= I191)
- binding benzamide: F145 (= F134), S146 (= S135), G147 (= G136), Q191 (≠ T185), G192 (= G186), G193 (= G187), A194 (≠ S188), W327 (vs. gap)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
37% identity, 53% coverage: 11:255/459 of query aligns to 8:251/487 of 1m21A
- active site: K81 (= K83), S160 (= S164), S161 (= S165), T179 (= T183), T181 (= T185), D182 (≠ G186), G183 (= G187), S184 (= S188), C187 (≠ I191)
- binding : A129 (= A133), N130 (vs. gap), F131 (= F134), C158 (≠ G162), G159 (= G163), S160 (= S164), S184 (= S188), C187 (≠ I191), I212 (≠ L216)
Sites not aligning to the query:
3kfuE Crystal structure of the transamidosome (see paper)
33% identity, 81% coverage: 74:445/459 of query aligns to 56:447/468 of 3kfuE
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
28% identity, 95% coverage: 11:445/459 of query aligns to 7:542/564 of 6te4A
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
27% identity, 95% coverage: 12:446/459 of query aligns to 9:467/490 of 4yjiA
- active site: K79 (= K83), S158 (= S164), S159 (= S165), G179 (≠ T185), G180 (= G186), G181 (= G187), A182 (≠ S188)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L85), G132 (≠ A133), S158 (= S164), G179 (≠ T185), G180 (= G186), A182 (≠ S188)
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
37% identity, 40% coverage: 73:254/459 of query aligns to 28:206/450 of 4n0iA
- active site: K38 (= K83), S116 (= S164), S117 (= S165), T135 (= T183), T137 (= T185), G138 (= G186), G139 (= G187), S140 (= S188), L143 (≠ I191)
- binding glutamine: G89 (≠ S135), T137 (= T185), G138 (= G186), S140 (= S188), Y168 (≠ L216)
Sites not aligning to the query:
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
34% identity, 59% coverage: 60:331/459 of query aligns to 43:294/412 of 1o9oA
- active site: K62 (= K83), A131 (≠ S164), S132 (= S165), T150 (= T183), T152 (= T185), G153 (= G186), G154 (= G187), S155 (= S188), R158 (≠ I191)
- binding 3-amino-3-oxopropanoic acid: G130 (≠ R151), T152 (= T185), G153 (= G186), G154 (= G187), S155 (= S188), R158 (≠ I191)
Sites not aligning to the query:
2wapA 3d-crystal structure of humanized-rat fatty acid amide hydrolase (faah) conjugated with the drug-like urea inhibitor pf-3845 (see paper)
38% identity, 30% coverage: 75:212/459 of query aligns to 102:233/541 of 2wapA
- active site: K110 (= K83), S185 (= S164), S186 (= S165), T204 (= T183), I206 (≠ T185), G207 (= G186), G208 (= G187), S209 (= S188), F212 (≠ I191)
- binding 4-(3-{[5-(trifluoromethyl)pyridin-2-yl]oxy}benzyl)piperidine-1-carboxylic acid: F160 (= F134), S161 (= S135), I206 (≠ T185), G207 (= G186), S209 (= S188)
Sites not aligning to the query:
Query Sequence
>H281DRAFT_03959 FitnessBrowser__Burk376:H281DRAFT_03959
MATEFTPFPPLAQLAADLAAGRTTSRALVETALERIADPAGQGAVAFMHVDADGARQAAD
AHDRLRAAGTVLSPLAGIPVSVKDLFDIEGQPTRAGSTVLADAPAATQDAVAVARLKRAG
AVIVGRTNMSEFAFSGLGLNPHYGNPLSPYRRDVKGDERISGGSSSGAAASVADGMAAVA
LGTDTGGSLRIPAALCGLTGFKPTAARVPKQGGVPLSPTLDSFGPIGVSVACCALVDRML
AGLEPRVPAARPLEGVRLGVLTNYVTDGVEPEVAAAVDTALKHLEAAGAIVSEVRFASLD
RLPDINRFGFSPIEAYAWHRPLLEKHREQYDPRVLVRILKGQPASAADYLDLLAERDAML
AEAARTLWQRFDAVVAPTVPMLPPRVAELVSDDDLFGRTNALMLRNPGVFNFLDACALSL
PCHLRGDAPVGLMLAGAPHADDALLAIGRGAEAVLNAIR
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