SitesBLAST
Comparing HSERO_RS23305 FitnessBrowser__HerbieS:HSERO_RS23305 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)
47% identity, 98% coverage: 5:483/488 of query aligns to 7:479/485 of 2f2aA
- active site: K79 (= K74), S154 (= S149), S155 (= S150), S173 (≠ T168), T175 (= T170), G176 (= G171), G177 (= G172), S178 (= S173), Q181 (= Q176)
- binding glutamine: G130 (= G125), S154 (= S149), D174 (= D169), T175 (= T170), G176 (= G171), S178 (= S173), F206 (= F201), Y309 (= Y304), Y310 (= Y305), R358 (= R353), D425 (= D424)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
47% identity, 98% coverage: 5:483/488 of query aligns to 7:479/485 of 2dqnA
- active site: K79 (= K74), S154 (= S149), S155 (= S150), S173 (≠ T168), T175 (= T170), G176 (= G171), G177 (= G172), S178 (= S173), Q181 (= Q176)
- binding asparagine: M129 (= M124), G130 (= G125), T175 (= T170), G176 (= G171), S178 (= S173), Y309 (= Y304), Y310 (= Y305), R358 (= R353), D425 (= D424)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
47% identity, 100% coverage: 1:487/488 of query aligns to 2:476/478 of 3h0mA
- active site: K72 (= K74), S147 (= S149), S148 (= S150), S166 (≠ T168), T168 (= T170), G169 (= G171), G170 (= G172), S171 (= S173), Q174 (= Q176)
- binding glutamine: M122 (= M124), G123 (= G125), D167 (= D169), T168 (= T170), G169 (= G171), G170 (= G172), S171 (= S173), F199 (= F201), Y302 (= Y304), R351 (= R353), D418 (= D424)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
47% identity, 100% coverage: 1:487/488 of query aligns to 2:476/478 of 3h0lA
- active site: K72 (= K74), S147 (= S149), S148 (= S150), S166 (≠ T168), T168 (= T170), G169 (= G171), G170 (= G172), S171 (= S173), Q174 (= Q176)
- binding asparagine: G123 (= G125), S147 (= S149), G169 (= G171), G170 (= G172), S171 (= S173), Y302 (= Y304), R351 (= R353), D418 (= D424)
3kfuE Crystal structure of the transamidosome (see paper)
46% identity, 98% coverage: 8:487/488 of query aligns to 4:465/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
36% identity, 83% coverage: 66:471/488 of query aligns to 30:444/450 of 4n0iA
- active site: K38 (= K74), S116 (= S149), S117 (= S150), T135 (= T168), T137 (= T170), G138 (= G171), G139 (= G172), S140 (= S173), L143 (≠ Q176)
- binding glutamine: G89 (= G125), T137 (= T170), G138 (= G171), S140 (= S173), Y168 (≠ F201), Y271 (= Y304), Y272 (= Y305), R320 (= R353), D404 (= D424)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
33% identity, 85% coverage: 64:478/488 of query aligns to 85:498/508 of 3a1iA
- active site: K95 (= K74), S170 (= S149), S171 (= S150), G189 (≠ T168), Q191 (≠ T170), G192 (= G171), G193 (= G172), A194 (≠ S173), I197 (≠ Q176)
- binding benzamide: F145 (≠ M124), S146 (≠ G125), G147 (≠ S126), Q191 (≠ T170), G192 (= G171), G193 (= G172), A194 (≠ S173), W327 (≠ Y304)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
32% identity, 97% coverage: 1:474/488 of query aligns to 25:484/507 of Q84DC4
- T31 (≠ K7) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K74) mutation to A: Abolishes activity on mandelamide.
- S180 (= S149) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S150) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G171) 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 (= S173) mutation to A: Abolishes activity on mandelamide.
- Q207 (= Q176) 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 (= S300) 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 (≠ R352) 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 (≠ L428) 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.
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
31% identity, 97% coverage: 6:480/488 of query aligns to 8:479/487 of 1m21A
- active site: K81 (= K74), S160 (= S149), S161 (= S150), T179 (= T168), T181 (= T170), D182 (≠ G171), G183 (= G172), S184 (= S173), C187 (≠ Q176)
- binding : A129 (= A123), N130 (≠ M124), F131 (≠ G125), C158 (≠ G147), G159 (= G148), S160 (= S149), S184 (= S173), C187 (≠ Q176), I212 (≠ F201), R318 (≠ Y305), L321 (≠ A308), L365 (= L355), F426 (vs. gap)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
34% identity, 96% coverage: 10:477/488 of query aligns to 12:448/457 of 6c6gA
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
28% identity, 96% coverage: 12:478/488 of query aligns to 147:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A123), T258 (≠ S126), S281 (= S149), G302 (≠ T170), G303 (= G171), S305 (= S173), S472 (= S358), I532 (≠ D416), M539 (≠ A423)
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, 96% coverage: 12:478/488 of query aligns to 147:589/607 of Q7XJJ7
- K205 (= K74) mutation to A: Loss of activity.
- SS 281:282 (= SS 149:150) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 170:173) binding
- S305 (= S173) mutation to A: Loss of activity.
- R307 (= R175) mutation to A: Loss of activity.
- S360 (≠ F228) mutation to A: No effect.
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
27% identity, 99% coverage: 1:482/488 of query aligns to 3:478/490 of 4yjiA
- active site: K79 (= K74), S158 (= S149), S159 (= S150), G179 (≠ T170), G180 (= G171), G181 (= G172), A182 (≠ S173)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ I76), G132 (≠ A123), S158 (= S149), G179 (≠ T170), G180 (= G171), A182 (≠ S173)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
26% identity, 98% coverage: 3:478/488 of query aligns to 4:445/457 of 5h6sC
- active site: K77 (= K74), S152 (= S149), S153 (= S150), L173 (≠ T170), G174 (= G171), G175 (= G172), S176 (= S173)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A123), R128 (≠ G125), W129 (≠ S126), S152 (= S149), L173 (≠ T170), G174 (= G171), S176 (= S173), W306 (≠ Y304), F338 (≠ Y338)
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)
42% identity, 30% coverage: 66:213/488 of query aligns to 28:177/425 of Q9FR37
- K36 (= K74) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S149) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S150) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D169) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S173) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C181) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 214 S→T: Slightly reduces catalytic activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
31% identity, 89% coverage: 44:478/488 of query aligns to 44:439/461 of 4gysB
- active site: K72 (= K74), S146 (= S149), S147 (= S150), T165 (= T168), T167 (= T170), A168 (≠ G171), G169 (= G172), S170 (= S173), V173 (≠ Q176)
- binding malonate ion: A120 (= A123), G122 (= G125), S146 (= S149), T167 (= T170), A168 (≠ G171), S170 (= S173), S193 (≠ Y196), G194 (= G197), V195 (≠ M198), R200 (≠ S203), Y297 (≠ F319), R305 (= R327)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
27% identity, 89% coverage: 45:478/488 of query aligns to 62:462/605 of Q936X2
- K91 (= K74) mutation to A: Loss of activity.
- S165 (= S149) mutation to A: Loss of activity.
- S189 (= S173) mutation to A: Loss of activity.
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
31% identity, 50% coverage: 13:258/488 of query aligns to 14:259/482 of 3a2qA
- active site: K69 (= K74), S147 (= S149), S148 (= S150), N166 (≠ T168), A168 (≠ T170), A169 (≠ G171), G170 (= G172), A171 (≠ S173), I174 (≠ Q176)
- binding 6-aminohexanoic acid: G121 (≠ A123), G121 (≠ A123), N122 (≠ M124), S147 (= S149), A168 (≠ T170), A168 (≠ T170), A169 (≠ G171), A171 (≠ S173)
Sites not aligning to the query:
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
30% identity, 60% coverage: 4:296/488 of query aligns to 2:264/412 of 1o9oA
- active site: K62 (= K74), A131 (≠ S149), S132 (= S150), T150 (= T168), T152 (= T170), G153 (= G171), G154 (= G172), S155 (= S173), R158 (≠ Q176)
- binding 3-amino-3-oxopropanoic acid: G130 (= G148), T152 (= T170), G153 (= G171), G154 (= G172), S155 (= S173), R158 (≠ Q176)
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)
32% identity, 44% coverage: 4:216/488 of query aligns to 77:288/579 of Q9TUI8
- S217 (= S149) mutation to A: Loss of activity.
- S218 (= S150) mutation to A: Lowers activity by at least 98%.
- D237 (= D169) mutation D->E,N: Loss of activity.
- S241 (= S173) mutation to A: Loss of activity.
- C249 (= C181) mutation to A: Loss of activity.
Query Sequence
>HSERO_RS23305 FitnessBrowser__HerbieS:HSERO_RS23305
MHKLTLKELSAQLQARKISATELATLFLDRIDASDLNAFLHVDRELTLAQAKVADSRLSD
NNAGQLTGVPIAHKDIFVTRGWRTTAGSRMLDNYVSPFDATVVEQFNAAGMVTLGKLNCD
EFAMGSGNENSYFGPTLNPWDKRAVPGGSSGGSAAAVAARLAPAATATDTGGSIRQPASL
CGVTGIKPTYGSVSRYGMIAFASSLDQGGPIAKTAEDCGLLLNAMTGFDERDSTSLQRPK
EDFTRSLNDSLQGLRIGVPKEFFGAGLAADVEAAVRAALSEFEKLGAQLVEISLPKTELS
IPVYYVIAPAEASSNLSRFDGVRYGHRAADYGNLDDMYRKSRAEGFGEEVKRRILVGSYV
LSHGYYDAYYLQAQKIRRLIAQDFQNALAGANRQCDVIMGPVSPTVAWDLGDKTNDPVAN
YLADIFTLSTSLAGLPGMSIPCGFGQGEKNGKRPVGLQIIGNYFDEARLLNVAHQFQQAT
DWHLREPA
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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