SitesBLAST
Comparing BPHYT_RS28340 FitnessBrowser__BFirm:BPHYT_RS28340 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)
43% identity, 98% coverage: 11:482/484 of query aligns to 28:496/507 of Q84DC4
- T31 (= T14) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K83) mutation to A: Abolishes activity on mandelamide.
- S180 (= S160) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S161) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G182) 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 (= S184) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ I187) 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 (≠ N303) 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 (vs. gap) 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 (≠ L424) 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)
32% identity, 94% coverage: 18:474/484 of query aligns to 13:477/487 of 1m21A
- active site: K81 (= K83), S160 (= S160), S161 (= S161), T179 (= T179), T181 (= T181), D182 (≠ G182), G183 (= G183), S184 (= S184), C187 (≠ I187)
- binding : A129 (= A132), N130 (≠ F133), F131 (vs. gap), C158 (≠ G158), G159 (= G159), S160 (= S160), S184 (= S184), C187 (≠ I187), I212 (= I219), R318 (vs. gap), L321 (≠ A311), L365 (= L353), F426 (≠ V403)
3kfuE Crystal structure of the transamidosome (see paper)
35% identity, 83% coverage: 73:474/484 of query aligns to 55:455/468 of 3kfuE
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
29% identity, 89% coverage: 43:473/484 of query aligns to 39:473/485 of 2f2aA
- active site: K79 (= K83), S154 (= S160), S155 (= S161), S173 (≠ T179), T175 (= T181), G176 (= G182), G177 (= G183), S178 (= S184), Q181 (≠ I187)
- binding glutamine: G130 (= G134), S154 (= S160), D174 (= D180), T175 (= T181), G176 (= G182), S178 (= S184), F206 (≠ I219), Y309 (vs. gap), Y310 (vs. gap), R358 (≠ A347), D425 (= D421)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
29% identity, 89% coverage: 43:473/484 of query aligns to 39:473/485 of 2dqnA
- active site: K79 (= K83), S154 (= S160), S155 (= S161), S173 (≠ T179), T175 (= T181), G176 (= G182), G177 (= G183), S178 (= S184), Q181 (≠ I187)
- binding asparagine: M129 (≠ F133), G130 (= G134), T175 (= T181), G176 (= G182), S178 (= S184), Y309 (vs. gap), Y310 (vs. gap), R358 (≠ A347), D425 (= D421)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
31% identity, 85% coverage: 64:474/484 of query aligns to 50:467/478 of 3h0mA
- active site: K72 (= K83), S147 (= S160), S148 (= S161), S166 (≠ T179), T168 (= T181), G169 (= G182), G170 (= G183), S171 (= S184), Q174 (≠ I187)
- binding glutamine: M122 (≠ F133), G123 (= G134), D167 (= D180), T168 (= T181), G169 (= G182), G170 (= G183), S171 (= S184), F199 (≠ I219), Y302 (≠ G307), R351 (≠ A347), D418 (≠ N426)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
31% identity, 85% coverage: 64:474/484 of query aligns to 50:467/478 of 3h0lA
- active site: K72 (= K83), S147 (= S160), S148 (= S161), S166 (≠ T179), T168 (= T181), G169 (= G182), G170 (= G183), S171 (= S184), Q174 (≠ I187)
- binding asparagine: G123 (= G134), S147 (= S160), G169 (= G182), G170 (= G183), S171 (= S184), Y302 (≠ G307), R351 (≠ A347), D418 (≠ N426)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
29% identity, 83% coverage: 75:475/484 of query aligns to 197:590/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A132), T258 (≠ I135), S281 (= S160), G302 (≠ T181), G303 (= G182), S305 (= S184), S472 (= S354), I532 (≠ V409), M539 (= M420)
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, 83% coverage: 75:475/484 of query aligns to 197:590/607 of Q7XJJ7
- K205 (= K83) mutation to A: Loss of activity.
- SS 281:282 (= SS 160:161) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 181:184) binding
- S305 (= S184) mutation to A: Loss of activity.
- R307 (= R186) mutation to A: Loss of activity.
- S360 (≠ A246) 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, 47% coverage: 11:238/484 of query aligns to 1:221/457 of 6c6gA
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
32% identity, 89% coverage: 56:484/484 of query aligns to 48:457/461 of 4gysB
- active site: K72 (= K83), S146 (= S160), S147 (= S161), T165 (= T179), T167 (= T181), A168 (≠ G182), G169 (= G183), S170 (= S184), V173 (≠ I187)
- binding malonate ion: A120 (= A132), G122 (= G134), S146 (= S160), T167 (= T181), A168 (≠ G182), S170 (= S184), S193 (≠ D214), G194 (≠ A215), V195 (= V216), R200 (≠ H221), Y297 (≠ V306), R305 (vs. gap)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
29% identity, 97% coverage: 7:474/484 of query aligns to 1:445/457 of 5h6sC
- active site: K77 (= K83), S152 (= S160), S153 (= S161), L173 (≠ T181), G174 (= G182), G175 (= G183), S176 (= S184)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A132), R128 (≠ T136), W129 (≠ S137), S152 (= S160), L173 (≠ T181), G174 (= G182), S176 (= S184), W306 (≠ L320), F338 (≠ V352)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
29% identity, 88% coverage: 47:472/484 of query aligns to 56:460/605 of Q936X2
- K91 (= K83) mutation to A: Loss of activity.
- S165 (= S160) mutation to A: Loss of activity.
- S189 (= S184) mutation to A: Loss of activity.
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)
39% identity, 35% coverage: 75:243/484 of query aligns to 28:189/425 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 (= S160) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S161) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D180) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S184) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (≠ T192) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 214 S→T: Slightly reduces catalytic activity.
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
38% identity, 44% coverage: 75:289/484 of query aligns to 87:310/508 of 3a1iA
- active site: K95 (= K83), S170 (= S160), S171 (= S161), G189 (≠ T179), Q191 (≠ T181), G192 (= G182), G193 (= G183), A194 (≠ S184), I197 (= I187)
- binding benzamide: F145 (= F133), S146 (≠ G134), G147 (≠ I135), Q191 (≠ T181), G192 (= G182), G193 (= G183), A194 (≠ S184)
Sites not aligning to the query:
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
33% identity, 49% coverage: 7:243/484 of query aligns to 1:237/564 of 6te4A
Sites not aligning to the query:
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
38% identity, 33% coverage: 75:233/484 of query aligns to 30:182/450 of 4n0iA
- active site: K38 (= K83), S116 (= S160), S117 (= S161), T135 (= T179), T137 (= T181), G138 (= G182), G139 (= G183), S140 (= S184), L143 (≠ I187)
- binding glutamine: G89 (≠ T136), T137 (= T181), G138 (= G182), S140 (= S184), Y168 (≠ I219)
Sites not aligning to the query:
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
29% identity, 73% coverage: 120:474/484 of query aligns to 120:474/490 of 4yjiA
Sites not aligning to the query:
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
33% identity, 49% coverage: 9:245/484 of query aligns to 3:228/482 of 3a2qA
- active site: K69 (= K83), S147 (= S160), S148 (= S161), N166 (≠ T179), A168 (≠ T181), A169 (≠ G182), G170 (= G183), A171 (≠ S184), I174 (= I187)
- binding 6-aminohexanoic acid: G121 (≠ A132), G121 (≠ A132), N122 (≠ F133), S147 (= S160), A168 (≠ T181), A168 (≠ T181), A169 (≠ G182), A171 (≠ S184)
Sites not aligning to the query:
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
33% identity, 50% coverage: 74:315/484 of query aligns to 53:269/412 of 1o9oA
- active site: K62 (= K83), A131 (≠ S160), S132 (= S161), T150 (= T179), T152 (= T181), G153 (= G182), G154 (= G183), S155 (= S184), R158 (≠ I187)
- binding 3-amino-3-oxopropanoic acid: G130 (= G159), T152 (= T181), G153 (= G182), G154 (= G183), S155 (= S184), R158 (≠ I187)
Sites not aligning to the query:
Query Sequence
>BPHYT_RS28340 FitnessBrowser__BFirm:BPHYT_RS28340
MTWTVDEQLALSATEAVAAIQSGRLNAADYVATLLARAAALSSLNALTTLELDGALAAAR
RIDALPAAEKARLPLAGLPIVVKDNINTAGMQTSAGTPALAGFIPKTNAPSVQRLIDAGA
IVLGKANMHELAFGITSTNLATHAGPVRNPYDPSLIPGGSSGGTAAAIAARIVPAGLGTD
TGGSTRIPAALTGTVGFRPSVGNGGAERRYHDPDAVVPISHTRDTVGPMARTVADIALLD
GVITGAGALPVVALNGLRIGLPAPLWEGLERQVEDVARAALRQLEAAGVVFVPVAMSELD
DLNGMVGGPIAIHEARDDVLAWLVANDAPVKTVVEMAARIASPDVRAIYDGVLSDVLGDR
YEAALNHWRPRLQQYMAATFADERLDALLFPTTRLAAVPIDEVNGSSVVSVDGSAAIDTM
DAFLHNTDPASTSGIPGLSLPAGMTASGLPVGLELDGPLGEDRRLLAIGIAFEQLLGALP
APVL
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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