SitesBLAST
Comparing 8502127 FitnessBrowser__Miya:8502127 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)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
51% identity, 92% coverage: 12:473/501 of query aligns to 6:459/478 of 3h0mA
- active site: K72 (= K82), S147 (= S157), S148 (= S158), S166 (≠ T176), T168 (= T178), G169 (= G179), G170 (= G180), S171 (= S181), Q174 (= Q184)
- binding glutamine: M122 (= M132), G123 (= G133), D167 (= D177), T168 (= T178), G169 (= G179), G170 (= G180), S171 (= S181), F199 (≠ Y209), Y302 (= Y314), R351 (= R363), D418 (= D430)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
51% identity, 92% coverage: 12:473/501 of query aligns to 6:459/478 of 3h0lA
- active site: K72 (= K82), S147 (= S157), S148 (= S158), S166 (≠ T176), T168 (= T178), G169 (= G179), G170 (= G180), S171 (= S181), Q174 (= Q184)
- binding asparagine: G123 (= G133), S147 (= S157), G169 (= G179), G170 (= G180), S171 (= S181), Y302 (= Y314), R351 (= R363), D418 (= D430)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
50% identity, 91% coverage: 20:476/501 of query aligns to 15:469/485 of 2f2aA
- active site: K79 (= K82), S154 (= S157), S155 (= S158), S173 (≠ T176), T175 (= T178), G176 (= G179), G177 (= G180), S178 (= S181), Q181 (= Q184)
- binding glutamine: G130 (= G133), S154 (= S157), D174 (= D177), T175 (= T178), G176 (= G179), S178 (= S181), F206 (≠ Y209), Y309 (= Y314), Y310 (= Y315), R358 (= R363), D425 (= D430)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
50% identity, 91% coverage: 20:476/501 of query aligns to 15:469/485 of 2dqnA
- active site: K79 (= K82), S154 (= S157), S155 (= S158), S173 (≠ T176), T175 (= T178), G176 (= G179), G177 (= G180), S178 (= S181), Q181 (= Q184)
- binding asparagine: M129 (= M132), G130 (= G133), T175 (= T178), G176 (= G179), S178 (= S181), Y309 (= Y314), Y310 (= Y315), R358 (= R363), D425 (= D430)
3kfuE Crystal structure of the transamidosome (see paper)
50% identity, 92% coverage: 15:473/501 of query aligns to 4:446/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
35% identity, 83% coverage: 50:465/501 of query aligns to 6:435/450 of 4n0iA
- active site: K38 (= K82), S116 (= S157), S117 (= S158), T135 (= T176), T137 (= T178), G138 (= G179), G139 (= G180), S140 (= S181), L143 (≠ Q184)
- binding glutamine: G89 (= G133), T137 (= T178), G138 (= G179), S140 (= S181), Y168 (= Y209), Y271 (= Y314), Y272 (= Y315), R320 (= R363), D404 (= D430)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
37% identity, 82% coverage: 74:486/501 of query aligns to 87:506/508 of 3a1iA
- active site: K95 (= K82), S170 (= S157), S171 (= S158), G189 (≠ T176), Q191 (≠ T178), G192 (= G179), G193 (= G180), A194 (≠ S181), I197 (≠ Q184)
- binding benzamide: F145 (≠ M132), S146 (≠ G133), G147 (≠ S134), Q191 (≠ T178), G192 (= G179), G193 (= G180), A194 (≠ S181), W327 (≠ Y314)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
35% identity, 94% coverage: 11:480/501 of query aligns to 1:448/457 of 6c6gA
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
35% identity, 93% coverage: 13:476/501 of query aligns to 8:472/487 of 1m21A
- active site: K81 (= K82), S160 (= S157), S161 (= S158), T179 (= T176), T181 (= T178), D182 (≠ G179), G183 (= G180), S184 (= S181), C187 (≠ Q184)
- binding : A129 (= A131), N130 (≠ M132), F131 (≠ G133), C158 (≠ G155), G159 (= G156), S160 (= S157), S184 (= S181), C187 (≠ Q184), I212 (≠ Y209), R318 (≠ Y315), L321 (≠ A318), L365 (≠ M365), F426 (vs. gap)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
31% identity, 81% coverage: 69:476/501 of query aligns to 192:584/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A131), T258 (≠ S134), S281 (= S157), G302 (≠ T178), G303 (= G179), S305 (= S181), S472 (≠ L347), I532 (vs. gap), M539 (≠ L424)
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)
31% identity, 81% coverage: 69:476/501 of query aligns to 192:584/607 of Q7XJJ7
- K205 (= K82) mutation to A: Loss of activity.
- SS 281:282 (= SS 157:158) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 178:181) binding
- S305 (= S181) mutation to A: Loss of activity.
- R307 (= R183) mutation to A: Loss of activity.
- S360 (≠ H236) mutation to A: No effect.
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
30% identity, 95% coverage: 11:484/501 of query aligns to 28:491/507 of Q84DC4
- T31 (≠ A14) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K82) mutation to A: Abolishes activity on mandelamide.
- S180 (= S157) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S158) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G179) 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 (= S181) mutation to A: Abolishes activity on mandelamide.
- Q207 (= Q184) 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 (= S310) 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 (≠ Y369) 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 (≠ S435) 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.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
32% identity, 91% coverage: 26:483/501 of query aligns to 17:441/461 of 4gysB
- active site: K72 (= K82), S146 (= S157), S147 (= S158), T165 (= T176), T167 (= T178), A168 (≠ G179), G169 (= G180), S170 (= S181), V173 (≠ Q184)
- binding malonate ion: A120 (= A131), G122 (= G133), S146 (= S157), T167 (= T178), A168 (≠ G179), S170 (= S181), S193 (≠ F204), G194 (= G205), V195 (≠ L206), R200 (≠ S211), Y297 (≠ F329), R305 (= R337)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
34% identity, 80% coverage: 71:470/501 of query aligns to 80:451/605 of Q936X2
- K91 (= K82) mutation to A: Loss of activity.
- S165 (= S157) mutation to A: Loss of activity.
- S189 (= S181) mutation to A: Loss of activity.
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
28% identity, 93% coverage: 11:475/501 of query aligns to 5:439/457 of 5h6sC
- active site: K77 (= K82), S152 (= S157), S153 (= S158), L173 (≠ T178), G174 (= G179), G175 (= G180), S176 (= S181)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A131), R128 (≠ G133), W129 (≠ S134), S152 (= S157), L173 (≠ T178), G174 (= G179), S176 (= S181), W306 (≠ Y314), F338 (≠ L366)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
29% identity, 93% coverage: 12:476/501 of query aligns to 7:469/490 of 4yjiA
- active site: K79 (= K82), S158 (= S157), S159 (= S158), G179 (≠ T178), G180 (= G179), G181 (= G180), A182 (≠ S181)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (vs. gap), G132 (≠ A131), S158 (= S157), G179 (≠ T178), G180 (= G179), A182 (≠ S181)
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
28% identity, 93% coverage: 8:473/501 of query aligns to 2:542/564 of 6te4A
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
37% identity, 49% coverage: 24:268/501 of query aligns to 18:259/482 of 3a2qA
- active site: K69 (= K82), S147 (= S157), S148 (= S158), N166 (≠ T176), A168 (≠ T178), A169 (≠ G179), G170 (= G180), A171 (≠ S181), I174 (≠ Q184)
- binding 6-aminohexanoic acid: G121 (≠ A131), G121 (≠ A131), N122 (≠ M132), S147 (= S157), A168 (≠ T178), A168 (≠ T178), A169 (≠ G179), A171 (≠ S181)
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, 94% coverage: 11:483/501 of query aligns to 2:410/412 of 1o9oA
- active site: K62 (= K82), A131 (≠ S157), S132 (= S158), T150 (= T176), T152 (= T178), G153 (= G179), G154 (= G180), S155 (= S181), R158 (≠ Q184)
- binding 3-amino-3-oxopropanoic acid: G130 (= G156), T152 (= T178), G153 (= G179), G154 (= G180), S155 (= S181), R158 (≠ Q184), P359 (= P423)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
30% identity, 94% coverage: 11:483/501 of query aligns to 2:410/412 of 1ocmA
- active site: K62 (= K82), S131 (= S157), S132 (= S158), T152 (= T178), G153 (= G179), G154 (= G180), S155 (= S181)
- binding pyrophosphate 2-: R113 (≠ G133), S131 (= S157), Q151 (≠ D177), T152 (= T178), G153 (= G179), G154 (= G180), S155 (= S181), R158 (≠ Q184), P359 (= P423)
Query Sequence
>8502127 FitnessBrowser__Miya:8502127
MSDTSTAIVSLSLAEVRDRLARRELTAEQVTAACLDRITATEPAIAALLVTRGEGALAEA
RALDAAGPDPAKPLWGVPLTVKDALTTAGTRTTCGSRILGDFTPHYDAFAVGKLREAGAV
ILGKTNMDEFAMGSSTENSAFGPTRNPWNVARVPGGSSGGSAASVAAGQCFGSLGTDTGG
SIRQPASLCGCVGLKPTYGRVSRFGLVAYGSSLDQIGPLTRTVEDAALLLSVIAGHDPRD
ATSATLPVDDYMGALASRKDLSGVRIGVPREFRGEGIDPEVSAACEAALDTARGLGATIV
DVELPHTPYSIAAYYIIAPAEASSNLARFDGVRYGRRAESPRDLADLYVRSRAEGFGDEV
QRRIMLGTYVLSSGYYDAYYRKAAQVRRLIREDYEKALSRCDVLCGPASPVTAWGLGELT
SDPLKMYMMDVFTLSLNLAGLPGLCIPVGMGSRSGMPVGLQMLGRAFGEGDLLAAANVLS
GALGVPGVAPAISAAAAGAGA
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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