SitesBLAST
Comparing H281DRAFT_01685 FitnessBrowser__Burk376:H281DRAFT_01685 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)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
29% identity, 99% coverage: 5:469/469 of query aligns to 3:485/485 of 2f2aA
- active site: K79 (= K80), S154 (= S155), S155 (= S156), S173 (≠ T174), T175 (≠ L176), G176 (≠ A177), G177 (≠ I178), S178 (= S179), Q181 (≠ G182)
- binding glutamine: G130 (≠ W131), S154 (= S155), D174 (= D175), T175 (≠ L176), G176 (≠ A177), S178 (= S179), F206 (≠ R207), Y309 (≠ F312), Y310 (≠ N313), R358 (vs. gap), D425 (vs. gap)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
29% identity, 99% coverage: 5:469/469 of query aligns to 3:485/485 of 2dqnA
- active site: K79 (= K80), S154 (= S155), S155 (= S156), S173 (≠ T174), T175 (≠ L176), G176 (≠ A177), G177 (≠ I178), S178 (= S179), Q181 (≠ G182)
- binding asparagine: M129 (≠ Y130), G130 (≠ W131), T175 (≠ L176), G176 (≠ A177), S178 (= S179), Y309 (≠ F312), Y310 (≠ N313), R358 (vs. gap), D425 (vs. gap)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
31% identity, 96% coverage: 10:461/469 of query aligns to 7:448/457 of 5h6sC
- active site: K77 (= K80), S152 (= S155), S153 (= S156), L173 (= L176), G174 (≠ A177), G175 (≠ I178), S176 (= S179)
- binding 4-oxidanylbenzohydrazide: C126 (≠ S129), R128 (≠ W131), W129 (≠ I132), S152 (= S155), L173 (= L176), G174 (≠ A177), S176 (= S179), W306 (≠ A308), F338 (≠ A340)
3kfuE Crystal structure of the transamidosome (see paper)
32% identity, 96% coverage: 13:460/469 of query aligns to 1:457/468 of 3kfuE
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
31% identity, 98% coverage: 3:461/469 of query aligns to 1:477/490 of 4yjiA
- active site: K79 (= K80), S158 (= S155), S159 (= S156), G179 (≠ L176), G180 (≠ A177), G181 (≠ I178), A182 (≠ S179)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ S82), G132 (≠ S129), S158 (= S155), G179 (≠ L176), G180 (≠ A177), A182 (≠ S179)
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, 96% coverage: 18:465/469 of query aligns to 139:596/607 of Q7XJJ7
- K205 (= K80) mutation to A: Loss of activity.
- SS 281:282 (= SS 155:156) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ LAIS 176:179) binding
- S305 (= S179) mutation to A: Loss of activity.
- R307 (= R181) mutation to A: Loss of activity.
- S360 (≠ P235) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
28% identity, 96% coverage: 18:465/469 of query aligns to 139:596/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ S129), T258 (≠ I132), S281 (= S155), G302 (≠ L176), G303 (≠ A177), S305 (= S179), S472 (≠ T342), I532 (≠ F395), M539 (≠ V402)
Sites not aligning to the query:
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 96% coverage: 8:457/469 of query aligns to 5:466/478 of 3h0mA
- active site: K72 (= K80), S147 (= S155), S148 (= S156), S166 (≠ T174), T168 (≠ L176), G169 (≠ A177), G170 (≠ I178), S171 (= S179), Q174 (≠ G182)
- binding glutamine: M122 (≠ Y130), G123 (≠ W131), D167 (= D175), T168 (≠ L176), G169 (≠ A177), G170 (≠ I178), S171 (= S179), F199 (≠ R207), Y302 (≠ F312), R351 (≠ K352), D418 (≠ G409)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 96% coverage: 8:457/469 of query aligns to 5:466/478 of 3h0lA
- active site: K72 (= K80), S147 (= S155), S148 (= S156), S166 (≠ T174), T168 (≠ L176), G169 (≠ A177), G170 (≠ I178), S171 (= S179), Q174 (≠ G182)
- binding asparagine: G123 (≠ W131), S147 (= S155), G169 (≠ A177), G170 (≠ I178), S171 (= S179), Y302 (≠ F312), R351 (≠ K352), D418 (≠ G409)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
30% identity, 94% coverage: 21:463/469 of query aligns to 19:482/487 of 1m21A
- active site: K81 (= K80), S160 (= S155), S161 (= S156), T179 (= T174), T181 (≠ L176), D182 (≠ A177), G183 (≠ I178), S184 (= S179), C187 (≠ G182)
- binding : A129 (≠ S129), N130 (≠ Y130), F131 (≠ W131), C158 (≠ G153), G159 (= G154), S160 (= S155), S184 (= S179), C187 (≠ G182), I212 (≠ R207), R318 (vs. gap), L321 (vs. gap), L365 (vs. gap), F426 (≠ I397)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
31% identity, 99% coverage: 6:469/469 of query aligns to 3:480/482 of 3a2qA
- active site: K69 (= K80), S147 (= S155), S148 (= S156), N166 (≠ T174), A168 (≠ L176), A169 (= A177), G170 (≠ I178), A171 (≠ S179), I174 (≠ G182)
- binding 6-aminohexanoic acid: G121 (≠ S129), G121 (≠ S129), N122 (≠ Y130), S147 (= S155), A168 (≠ L176), A168 (≠ L176), A169 (= A177), A171 (≠ S179), C313 (≠ L315)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
31% identity, 83% coverage: 70:459/469 of query aligns to 85:499/508 of 3a1iA
- active site: K95 (= K80), S170 (= S155), S171 (= S156), G189 (≠ T174), Q191 (≠ L176), G192 (≠ A177), G193 (≠ I178), A194 (≠ S179), I197 (≠ G182)
- binding benzamide: F145 (≠ Y130), S146 (≠ W131), G147 (≠ I132), Q191 (≠ L176), G192 (≠ A177), G193 (≠ I178), A194 (≠ S179), W327 (≠ L315)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
31% identity, 96% coverage: 13:463/469 of query aligns to 6:454/457 of 6c6gA
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
28% identity, 96% coverage: 11:459/469 of query aligns to 31:489/507 of Q84DC4
- T31 (= T11) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K80) mutation to A: Abolishes activity on mandelamide.
- S180 (= S155) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S156) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ A177) 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 (= S179) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ G182) 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 (≠ D306) 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 (= Q359) 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 (≠ L407) 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.
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
36% identity, 45% coverage: 13:225/469 of query aligns to 10:229/564 of 6te4A
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)
34% identity, 54% coverage: 12:264/469 of query aligns to 81:329/579 of Q9TUI8
- S217 (= S155) mutation to A: Loss of activity.
- S218 (= S156) mutation to A: Lowers activity by at least 98%.
- D237 (= D175) mutation D->E,N: Loss of activity.
- S241 (= S179) mutation to A: Loss of activity.
- C249 (≠ T187) mutation to A: Loss of activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
37% identity, 45% coverage: 50:258/469 of query aligns to 45:255/461 of 4gysB
- active site: K72 (= K80), S146 (= S155), S147 (= S156), T165 (= T174), T167 (≠ L176), A168 (= A177), G169 (≠ I178), S170 (= S179), V173 (≠ G182)
- binding malonate ion: A120 (≠ S129), G122 (≠ W131), S146 (= S155), T167 (≠ L176), A168 (= A177), S170 (= S179), S193 (≠ T202), G194 (= G203), V195 (≠ I204), R200 (= R210)
Sites not aligning to the query:
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
29% identity, 95% coverage: 13:457/469 of query aligns to 4:407/412 of 1o9oA
- active site: K62 (= K80), A131 (≠ S155), S132 (= S156), T150 (= T174), T152 (≠ L176), G153 (≠ A177), G154 (≠ I178), S155 (= S179), R158 (≠ G182)
- binding 3-amino-3-oxopropanoic acid: G130 (= G154), T152 (≠ L176), G153 (≠ A177), G154 (≠ I178), S155 (= S179), R158 (≠ G182), P359 (≠ A404)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
29% identity, 95% coverage: 13:457/469 of query aligns to 4:407/412 of 1ocmA
- active site: K62 (= K80), S131 (= S155), S132 (= S156), T152 (≠ L176), G153 (≠ A177), G154 (≠ I178), S155 (= S179)
- binding pyrophosphate 2-: R113 (≠ W131), S131 (= S155), Q151 (≠ D175), T152 (≠ L176), G153 (≠ A177), G154 (≠ I178), S155 (= S179), R158 (≠ G182), P359 (≠ A404)
2wj1A 3d-crystal structure of humanized-rat fatty acid amide hydrolase (faah) conjugated with 7-phenyl-1-(4-(pyridin-2-yl)oxazol-2-yl) heptan- 1-one, an alpha-ketooxazole (see paper)
30% identity, 62% coverage: 21:313/469 of query aligns to 57:343/543 of 2wj1A
- active site: K109 (= K80), S184 (= S155), S185 (= S156), T203 (= T174), I205 (≠ L176), G206 (≠ A177), G207 (≠ I178), S208 (= S179), F211 (≠ G182)
- binding 7-phenyl-1-(4-pyridin-2-yl-1,3-oxazol-2-yl)heptane-1,1-diol: S157 (≠ F128), M158 (≠ S129), F159 (≠ Y130), S184 (= S155), T203 (= T174), D204 (= D175), I205 (≠ L176), G206 (≠ A177), S208 (= S179), C236 (vs. gap)
Sites not aligning to the query:
Query Sequence
>H281DRAFT_01685 FitnessBrowser__Burk376:H281DRAFT_01685
MSSEIFFQDATRLAELIRKREISPVEVMQAHLDRIEAIDPKVNAIVTVADDVMKAAQAAE
AAVLAGQTLGPLHGVPFTAKDSIDTAGVPTQRGSPIFKGRVPDADAVSVARLKKAGGILL
AKTNLPEFSYWIESDNLLSGRSNNPWDLDLTPGGSSGGESAAIAAGMSPLGLGTDLAISV
RGPAAQTGIVSLKATHGRVPMTGIWPRAPRRFWHVGPMARSIRDLALAFSQLAGPDGQDA
FASSTVQFDAGVVRSDDRPLRVGWMVGPGFGPVDPEVAATVQSAAEALRSVGCIVEPVSI
PALERDFALDVFNRLHVMEMKPAFAEATAGHAQDELYKMARTMLALPDTSMKDYIDAEQA
AERLRDGYAEYFTRYDALITHVLPIPAHKHGVDTFTINGETVDARYLQGATVPLNVTGLP
GVSMRFGTSKDALPINVQIVGSWQAESTILHIASLLESVSPVRDQHPKI
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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