SitesBLAST
Comparing Pf6N2E2_878 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_878 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)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
49% identity, 98% coverage: 2:496/504 of query aligns to 1:497/508 of 3a1iA
- active site: K95 (= K96), S170 (= S171), S171 (= S172), G189 (= G190), Q191 (= Q192), G192 (= G193), G193 (= G194), A194 (≠ S195), I197 (= I198)
- binding benzamide: F145 (≠ L146), S146 (= S147), G147 (= G148), Q191 (= Q192), G192 (= G193), G193 (= G194), A194 (≠ S195), W327 (= W327)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
35% identity, 82% coverage: 86:496/504 of query aligns to 69:473/485 of 2f2aA
- active site: K79 (= K96), S154 (= S171), S155 (= S172), S173 (≠ G190), T175 (≠ Q192), G176 (= G193), G177 (= G194), S178 (= S195), Q181 (≠ I198)
- binding glutamine: G130 (≠ S147), S154 (= S171), D174 (= D191), T175 (≠ Q192), G176 (= G193), S178 (= S195), F206 (≠ I223), Y309 (≠ W327), Y310 (≠ S328), R358 (≠ C378), D425 (vs. gap)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
35% identity, 82% coverage: 86:496/504 of query aligns to 69:473/485 of 2dqnA
- active site: K79 (= K96), S154 (= S171), S155 (= S172), S173 (≠ G190), T175 (≠ Q192), G176 (= G193), G177 (= G194), S178 (= S195), Q181 (≠ I198)
- binding asparagine: M129 (≠ L146), G130 (≠ S147), T175 (≠ Q192), G176 (= G193), S178 (= S195), Y309 (≠ W327), Y310 (≠ S328), R358 (≠ C378), D425 (vs. gap)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
33% identity, 81% coverage: 88:496/504 of query aligns to 64:466/478 of 3h0mA
- active site: K72 (= K96), S147 (= S171), S148 (= S172), S166 (≠ G190), T168 (≠ Q192), G169 (= G193), G170 (= G194), S171 (= S195), Q174 (≠ I198)
- binding glutamine: M122 (≠ L146), G123 (≠ S147), D167 (= D191), T168 (≠ Q192), G169 (= G193), G170 (= G194), S171 (= S195), F199 (≠ I223), Y302 (≠ W327), R351 (≠ C378), D418 (vs. gap)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
33% identity, 81% coverage: 88:496/504 of query aligns to 64:466/478 of 3h0lA
- active site: K72 (= K96), S147 (= S171), S148 (= S172), S166 (≠ G190), T168 (≠ Q192), G169 (= G193), G170 (= G194), S171 (= S195), Q174 (≠ I198)
- binding asparagine: G123 (≠ S147), S147 (= S171), G169 (= G193), G170 (= G194), S171 (= S195), Y302 (≠ W327), R351 (≠ C378), D418 (vs. gap)
3kfuE Crystal structure of the transamidosome (see paper)
34% identity, 81% coverage: 88:496/504 of query aligns to 57:454/468 of 3kfuE
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
32% identity, 82% coverage: 88:502/504 of query aligns to 73:482/487 of 1m21A
- active site: K81 (= K96), S160 (= S171), S161 (= S172), T179 (≠ G190), T181 (≠ Q192), D182 (≠ G193), G183 (= G194), S184 (= S195), C187 (≠ I198)
- binding : A129 (≠ C145), N130 (≠ L146), F131 (≠ S147), C158 (≠ G169), G159 (= G170), S160 (= S171), S184 (= S195), C187 (≠ I198), I212 (= I223), R318 (≠ C332), L321 (= L335), L365 (≠ F384), F426 (≠ E432)
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
30% identity, 81% coverage: 88:496/504 of query aligns to 197:588/607 of Q7XJJ7
- K205 (= K96) mutation to A: Loss of activity.
- SS 281:282 (= SS 171:172) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ QGGS 192:195) binding
- S305 (= S195) mutation to A: Loss of activity.
- R307 (= R197) mutation to A: Loss of activity.
- S360 (≠ A250) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
30% identity, 81% coverage: 88:496/504 of query aligns to 197:588/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ C145), T258 (≠ G148), S281 (= S171), G302 (≠ Q192), G303 (= G193), S305 (= S195), S472 (≠ Q383), I532 (≠ V441), M539 (≠ L448)
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)
30% identity, 73% coverage: 135:501/504 of query aligns to 122:478/490 of 4yjiA
Sites not aligning to the query:
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
37% identity, 39% coverage: 88:286/504 of query aligns to 66:265/457 of 6c6gA
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
26% identity, 82% coverage: 86:496/504 of query aligns to 67:444/457 of 5h6sC
- active site: K77 (= K96), S152 (= S171), S153 (= S172), L173 (≠ Q192), G174 (= G193), G175 (= G194), S176 (= S195)
- binding 4-oxidanylbenzohydrazide: C126 (= C145), R128 (≠ S147), W129 (≠ G148), S152 (= S171), L173 (≠ Q192), G174 (= G193), S176 (= S195), W306 (= W327), F338 (≠ V381)
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
25% identity, 85% coverage: 63:488/504 of query aligns to 8:442/450 of 4n0iA
- active site: K38 (= K96), S116 (= S171), S117 (= S172), T135 (≠ G190), T137 (≠ Q192), G138 (= G193), G139 (= G194), S140 (= S195), L143 (≠ I198)
- binding glutamine: G89 (≠ S147), T137 (≠ Q192), G138 (= G193), S140 (= S195), Y168 (≠ I223), Y271 (≠ W327), Y272 (≠ S328), R320 (≠ C378), D404 (≠ T440)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
26% identity, 81% coverage: 88:497/504 of query aligns to 92:488/507 of Q84DC4
- K100 (= K96) mutation to A: Abolishes activity on mandelamide.
- S180 (= S171) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S172) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G193) 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 (= S195) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ I198) 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 (≠ A323) 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 (= Q398) 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 (≠ L448) 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.
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
29% identity, 79% coverage: 84:481/504 of query aligns to 50:392/412 of 1o9oA
- active site: K62 (= K96), A131 (≠ S171), S132 (= S172), T150 (≠ G190), T152 (≠ Q192), G153 (= G193), G154 (= G194), S155 (= S195), R158 (≠ I198)
- binding 3-amino-3-oxopropanoic acid: G130 (= G170), T152 (≠ Q192), G153 (= G193), G154 (= G194), S155 (= S195), R158 (≠ I198), P359 (≠ E439)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
29% identity, 79% coverage: 84:481/504 of query aligns to 50:392/412 of 1ocmA
- active site: K62 (= K96), S131 (= S171), S132 (= S172), T152 (≠ Q192), G153 (= G193), G154 (= G194), S155 (= S195)
- binding pyrophosphate 2-: R113 (≠ S153), S131 (= S171), Q151 (≠ D191), T152 (≠ Q192), G153 (= G193), G154 (= G194), S155 (= S195), R158 (≠ I198), P359 (≠ E439)
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)
41% identity, 25% coverage: 122:246/504 of query aligns to 64:185/425 of Q9FR37
- S113 (= S171) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S172) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D191) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S195) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C203) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 36 active site, Charge relay system; K→A: Loss of catalytic activity.; K→R: Reduces catalytic activity 10-fold.
- 214 S→T: Slightly reduces catalytic activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
29% identity, 81% coverage: 83:488/504 of query aligns to 59:430/461 of 4gysB
- active site: K72 (= K96), S146 (= S171), S147 (= S172), T165 (≠ G190), T167 (≠ Q192), A168 (≠ G193), G169 (= G194), S170 (= S195), V173 (≠ I198)
- binding malonate ion: A120 (≠ C145), G122 (= G148), S146 (= S171), T167 (≠ Q192), A168 (≠ G193), S170 (= S195), S193 (≠ T218), G194 (= G219), V195 (= V220), R200 (≠ S225), Y297 (≠ W327), R305 (≠ G334)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
26% identity, 81% coverage: 88:495/504 of query aligns to 83:460/605 of Q936X2
- K91 (= K96) mutation to A: Loss of activity.
- S165 (= S171) mutation to A: Loss of activity.
- S189 (= S195) mutation to A: Loss of activity.
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
32% identity, 39% coverage: 84:281/504 of query aligns to 57:260/482 of 3a2qA
- active site: K69 (= K96), S147 (= S171), S148 (= S172), N166 (≠ G190), A168 (≠ Q192), A169 (≠ G193), G170 (= G194), A171 (≠ S195), I174 (= I198)
- binding 6-aminohexanoic acid: G121 (= G148), G121 (= G148), N122 (≠ G149), S147 (= S171), A168 (≠ Q192), A168 (≠ Q192), A169 (≠ G193), A171 (≠ S195)
Sites not aligning to the query:
Query Sequence
>Pf6N2E2_878 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_878
MAIIRPTLEHVQDLASRLHIQLTPEQASEYLALMQSSFDAYDLVDELPDFIPPVRYERSA
GYRPSSTDNPLNAWYYRTEVMGASSGKLSGKTVALKDNISLAGVPMMNGAAPLEGFVPSF
DATVVTRLLDAGATILGKATCEHYCLSGGSHTSDPAPVHNPFRHGYTTGGSSSGSAALVA
TGAVDLAIGGDQGGSIRIPAAWCGIYGMKPTWGLVPYTGVMAIESTFDHVGPMTSNVRDN
ALMLEVMAGADGLDPRQAAPKVDAYCDYLERGVTGLRIGVLQEGFQLANQDPRIAEKVRS
AIARLEALGARVEEVSVPEHNLAGSLWSPIGCEGLTMQMMHGNGAGFNWKGLYDVGLLDK
QAGWRDQANALSPSLKLCMFVGQFGLERYNGRYYAKAQNIARFARAAYDKALDTYDLLVM
PTVPITAQPLPEPGSSITETVTRALEMLGNTAAQDITGHPAMSIPCGLVDGLPVGLMLVG
RHYAEGTLYQAAAAFEASVDWRTL
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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