SitesBLAST
Comparing WP_085124903.1 NCBI__GCF_900177295.1:WP_085124903.1 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)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
35% identity, 93% coverage: 12:427/446 of query aligns to 14:443/457 of 6c6gA
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)
29% identity, 83% coverage: 65:435/446 of query aligns to 28:425/425 of Q9FR37
- K36 (= K73) 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 (≠ T150) 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 (≠ N181) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (≠ G248) mutation to T: Slightly reduces catalytic activity.
Q9AHE8 Urethanase; Enantioselective amidase; Ethyl carbamate-degrading amidase; EC 3.5.1.75 from Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium radiobacter) (see 3 papers)
28% identity, 80% coverage: 64:421/446 of query aligns to 89:498/517 of Q9AHE8
- R94 (≠ T69) mutation to P: No change in activity.
- I97 (= I72) mutation to L: 1.12-fold increase in specific activity toward ethyl carbamate, shows higher ethanol tolerance. 3.1-fold increase in specific activity toward ethyl carbamate and 1.5-fold increase in ethanol tolerance, shows lower pH tolerance; when associated with A-195.
- K98 (= K73) mutation to A: Almost loss of activity.
- P163 (≠ S139) mutation to A: Decrease in activity.
- A172 (≠ G148) mutation to G: Changes substrate specificity. Decrease in activity.
- S173 (= S149) mutation to A: Almost loss of activity.
- N175 (≠ S151) mutation to G: Decrease in activity.; mutation to S: Changes substrate specificity.
- G195 (= G171) mutation to A: 1.86-fold increase in specific activity toward ethyl carbamate, shows lower pH tolerance, causes a decrease in the thermostability. 3.1-fold increase in specific activity toward ethyl carbamate and 1.5-fold increase in ethanol tolerance, shows lower pH tolerance; when associated with L-97.
- S197 (= S173) mutation to A: Almost loss of activity.
- L200 (≠ V176) mutation to C: Decrease in activity.
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
32% identity, 90% coverage: 23:423/446 of query aligns to 30:464/487 of 1m21A
- active site: K81 (= K73), S160 (= S149), S161 (≠ T150), T179 (≠ S168), T181 (= T170), D182 (≠ G171), G183 (= G172), S184 (= S173), C187 (≠ V176)
- binding : A129 (= A123), N130 (vs. gap), F131 (≠ Y124), C158 (≠ G147), G159 (= G148), S160 (= S149), S184 (= S173), C187 (≠ V176), I212 (≠ L201), R318 (= R292), L321 (≠ V295), L365 (≠ R323), F426 (= F376)
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
34% identity, 50% coverage: 8:228/446 of query aligns to 137:360/607 of Q7XJJ7
- K205 (= K73) mutation to A: Loss of activity.
- SS 281:282 (≠ ST 149:150) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 170:173) binding substrate
- S305 (= S173) mutation to A: Loss of activity.
- R307 (= R175) mutation to A: Loss of activity.
- S360 (≠ T228) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
34% identity, 50% coverage: 8:228/446 of query aligns to 137:360/616 of 6diiH
Sites not aligning to the query:
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
33% identity, 50% coverage: 8:228/446 of query aligns to 137:360/605 of 8ey9B
Sites not aligning to the query:
8ey1D Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with n-(3-oxododecanoyl)-l-homoserine lactone
33% identity, 50% coverage: 8:228/446 of query aligns to 137:360/605 of 8ey1D
Sites not aligning to the query:
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
33% identity, 60% coverage: 12:277/446 of query aligns to 41:305/507 of Q84DC4
- K100 (= K73) mutation to A: Abolishes activity on mandelamide.
- S180 (= S149) mutation to A: Significantly decreases activity on mandelamide.
- S181 (≠ T150) 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 (≠ V176) 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.
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.
- 316 S→N: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with H-207 and N-437.
- 382 Q→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.
- 437 I→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, 84% coverage: 37:412/446 of query aligns to 37:414/461 of 4gysB
- active site: K72 (= K73), S146 (= S149), S147 (≠ T150), T165 (≠ S168), T167 (= T170), A168 (≠ G171), G169 (= G172), S170 (= S173), V173 (= V176)
- binding malonate ion: A120 (= A123), G122 (≠ S125), S146 (= S149), T167 (= T170), A168 (≠ G171), S170 (= S173), S193 (≠ D196), G194 (= G197), V195 (= V198), R200 (≠ G203), Y297 (≠ N291), R305 (≠ A299)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
36% identity, 48% coverage: 63:276/446 of query aligns to 62:287/478 of 3h0mA
- active site: K72 (= K73), S147 (= S149), S148 (≠ T150), S166 (= S168), T168 (= T170), G169 (= G171), G170 (= G172), S171 (= S173), Q174 (≠ V176)
- binding glutamine: M122 (≠ Y124), G123 (≠ S125), D167 (= D169), T168 (= T170), G169 (= G171), G170 (= G172), S171 (= S173), F199 (≠ L201)
Sites not aligning to the query:
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
36% identity, 48% coverage: 63:276/446 of query aligns to 62:287/478 of 3h0lA
- active site: K72 (= K73), S147 (= S149), S148 (≠ T150), S166 (= S168), T168 (= T170), G169 (= G171), G170 (= G172), S171 (= S173), Q174 (≠ V176)
- binding asparagine: G123 (≠ S125), S147 (= S149), G169 (= G171), G170 (= G172), S171 (= S173)
Sites not aligning to the query:
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
29% identity, 74% coverage: 36:366/446 of query aligns to 41:408/485 of 2f2aA
- active site: K79 (= K73), S154 (= S149), S155 (≠ T150), S173 (= S168), T175 (= T170), G176 (= G171), G177 (= G172), S178 (= S173), Q181 (≠ V176)
- binding glutamine: G130 (≠ S125), S154 (= S149), D174 (= D169), T175 (= T170), G176 (= G171), S178 (= S173), F206 (≠ L201), Y309 (vs. gap), Y310 (vs. gap), R358 (= R317)
Sites not aligning to the query:
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
29% identity, 74% coverage: 36:366/446 of query aligns to 41:408/485 of 2dqnA
- active site: K79 (= K73), S154 (= S149), S155 (≠ T150), S173 (= S168), T175 (= T170), G176 (= G171), G177 (= G172), S178 (= S173), Q181 (≠ V176)
- binding asparagine: M129 (≠ Y124), G130 (≠ S125), T175 (= T170), G176 (= G171), S178 (= S173), Y309 (vs. gap), Y310 (vs. gap), R358 (= R317)
Sites not aligning to the query:
Q9MUK5 Translocon at the outer membrane of chloroplasts 64 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
27% identity, 81% coverage: 67:427/446 of query aligns to 63:446/593 of Q9MUK5
Sites not aligning to the query:
- 516 N→A: Loss of HSP90 binding, but no effect on HSP70 binding.
- 550 R→A: 80% decrease of HSP70 and HSP90 binding.
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
29% identity, 81% coverage: 65:425/446 of query aligns to 87:490/508 of 3a1iA
- active site: K95 (= K73), S170 (= S149), S171 (≠ T150), G189 (≠ S168), Q191 (≠ T170), G192 (= G171), G193 (= G172), A194 (≠ S173), I197 (≠ V176)
- binding benzamide: F145 (≠ Y124), S146 (= S125), G147 (= G126), Q191 (≠ T170), G192 (= G171), G193 (= G172), A194 (≠ S173), W327 (≠ C290)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
31% identity, 82% coverage: 37:401/446 of query aligns to 54:429/605 of Q936X2
- K91 (= K73) mutation to A: Loss of activity.
- S165 (= S149) mutation to A: Loss of activity.
- S189 (= S173) mutation to A: Loss of activity.
3kfuE Crystal structure of the transamidosome (see paper)
41% identity, 48% coverage: 7:219/446 of query aligns to 8:210/468 of 3kfuE
Sites not aligning to the query:
9fz1A umg-sp3 (see paper)
38% identity, 46% coverage: 42:246/446 of query aligns to 44:252/438 of 9fz1A
Sites not aligning to the query:
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
31% identity, 82% coverage: 64:430/446 of query aligns to 53:412/412 of 1o9oA
- active site: K62 (= K73), A131 (≠ S149), S132 (≠ T150), T150 (≠ S168), T152 (= T170), G153 (= G171), G154 (= G172), S155 (= S173), R158 (≠ V176)
- binding 3-amino-3-oxopropanoic acid: G130 (= G148), T152 (= T170), G153 (= G171), G154 (= G172), S155 (= S173), R158 (≠ V176), P359 (≠ D377)
Query Sequence
>WP_085124903.1 NCBI__GCF_900177295.1:WP_085124903.1
MPLPPLRAQRLRLTARQRAERALERVAALPPLQLGRIFTALDPERILAAADAADARRAEG
EALPLHGLTVSIKDLFDEAGEITGAGSVELLSGVPAVADAEVVRRLKAAGAVPFGRTTMS
EFAYSGVGLNPHYGTCGNSRDPRRVPGGSTSGGAVGAALGLVEVALGSDTGGSVRVPAAL
NGLAGFKPSQAAVPLDGVFPLAGSYDSIGPLAGDIETCAEVHAVLSGTLGRVDREAGVRG
LRIGLLGGFLLDGLDAAVAADFEAALGRLARAGAELLPAEARFLEAAGRCNRAIVASEAH
AIHAGRMAALETSGDPRVLGRLRVAETLDRAEVEEACRLRAEAQGAWARLAAGFDLLVAP
TVPCVAPLIHDVARDFDRLNALVLRNTSAINFADGCAATLPMQAAGALPTGLMVCAANGA
DWACLDAAARIALLVCPAEGHCATAM
Or try a new SitesBLAST search
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