SitesBLAST
Comparing WP_011969923.1 NCBI__GCF_000017145.1:WP_011969923.1 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)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
32% identity, 91% coverage: 17:445/474 of query aligns to 15:473/485 of 2f2aA
- active site: K79 (= K81), S154 (= S156), S155 (= S157), S173 (= S175), T175 (= T177), G176 (= G178), G177 (= G179), S178 (= S180), Q181 (≠ S183)
- binding glutamine: G130 (≠ V132), S154 (= S156), D174 (= D176), T175 (= T177), G176 (= G178), S178 (= S180), F206 (≠ L208), Y309 (vs. gap), Y310 (vs. gap), R358 (≠ N336), D425 (≠ P397)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
32% identity, 91% coverage: 17:445/474 of query aligns to 15:473/485 of 2dqnA
- active site: K79 (= K81), S154 (= S156), S155 (= S157), S173 (= S175), T175 (= T177), G176 (= G178), G177 (= G179), S178 (= S180), Q181 (≠ S183)
- binding asparagine: M129 (= M131), G130 (≠ V132), T175 (= T177), G176 (= G178), S178 (= S180), Y309 (vs. gap), Y310 (vs. gap), R358 (≠ N336), D425 (≠ P397)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
30% identity, 92% coverage: 12:446/474 of query aligns to 9:467/478 of 3h0mA
- active site: K72 (= K81), S147 (= S156), S148 (= S157), S166 (= S175), T168 (= T177), G169 (= G178), G170 (= G179), S171 (= S180), Q174 (≠ S183)
- binding glutamine: M122 (= M131), G123 (≠ V132), D167 (= D176), T168 (= T177), G169 (= G178), G170 (= G179), S171 (= S180), F199 (≠ L208), Y302 (≠ G306), R351 (≠ N336), D418 (≠ P397)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
30% identity, 92% coverage: 12:446/474 of query aligns to 9:467/478 of 3h0lA
- active site: K72 (= K81), S147 (= S156), S148 (= S157), S166 (= S175), T168 (= T177), G169 (= G178), G170 (= G179), S171 (= S180), Q174 (≠ S183)
- binding asparagine: G123 (≠ V132), S147 (= S156), G169 (= G178), G170 (= G179), S171 (= S180), Y302 (≠ G306), R351 (≠ N336), D418 (≠ P397)
3kfuE Crystal structure of the transamidosome (see paper)
34% identity, 94% coverage: 12:457/474 of query aligns to 4:466/468 of 3kfuE
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
35% identity, 79% coverage: 71:446/474 of query aligns to 85:498/508 of 3a1iA
- active site: K95 (= K81), S170 (= S156), S171 (= S157), G189 (≠ S175), Q191 (≠ T177), G192 (= G178), G193 (= G179), A194 (≠ S180), I197 (≠ S183)
- binding benzamide: F145 (≠ M131), S146 (≠ V132), G147 (= G133), Q191 (≠ T177), G192 (= G178), G193 (= G179), A194 (≠ S180), W327 (≠ G306)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
34% identity, 93% coverage: 16:456/474 of query aligns to 14:485/487 of 1m21A
- active site: K81 (= K81), S160 (= S156), S161 (= S157), T179 (≠ S175), T181 (= T177), D182 (≠ G178), G183 (= G179), S184 (= S180), C187 (≠ S183)
- binding : A129 (= A130), N130 (≠ M131), F131 (≠ V132), C158 (≠ G154), G159 (= G155), S160 (= S156), S184 (= S180), C187 (≠ S183), I212 (≠ L208), R318 (≠ A307), L321 (≠ I310), L365 (≠ I337), F426 (= F388)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
30% identity, 79% coverage: 73:446/474 of query aligns to 197:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A130), T258 (≠ G133), S281 (= S156), G302 (≠ T177), G303 (= G178), S305 (= S180), S472 (= S330), I532 (≠ R394), M539 (≠ I401)
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)
30% identity, 79% coverage: 73:446/474 of query aligns to 197:589/607 of Q7XJJ7
- K205 (= K81) mutation to A: Loss of activity.
- SS 281:282 (= SS 156:157) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 177:180) binding substrate
- S305 (= S180) mutation to A: Loss of activity.
- R307 (= R182) mutation to A: Loss of activity.
- S360 (≠ A235) mutation to A: No effect.
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
30% identity, 79% coverage: 73:446/474 of query aligns to 197:589/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A130), G302 (≠ T177), G303 (= G178), G304 (= G179), A305 (≠ S180), V442 (≠ A307), I475 (≠ V333), M539 (≠ I401)
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
30% identity, 79% coverage: 73:446/474 of query aligns to 197:589/605 of 8ey1D
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
32% identity, 92% coverage: 8:445/474 of query aligns to 1:448/457 of 6c6gA
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
31% identity, 92% coverage: 12:446/474 of query aligns to 9:445/457 of 5h6sC
- active site: K77 (= K81), S152 (= S156), S153 (= S157), L173 (≠ T177), G174 (= G178), G175 (= G179), S176 (= S180)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A130), R128 (≠ V132), W129 (≠ G133), S152 (= S156), L173 (≠ T177), G174 (= G178), S176 (= S180), W306 (vs. gap), F338 (≠ L338)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
32% identity, 93% coverage: 3:445/474 of query aligns to 23:487/507 of Q84DC4
- T31 (≠ L11) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K81) mutation to A: Abolishes activity on mandelamide.
- S180 (= S156) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S157) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G178) 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 (= S180) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ S183) 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 (≠ V305) 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 (≠ R350) 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 (≠ T396) 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.
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
33% identity, 89% coverage: 16:435/474 of query aligns to 10:397/412 of 1ocmA
- active site: K62 (= K81), S131 (= S156), S132 (= S157), T152 (= T177), G153 (= G178), G154 (= G179), S155 (= S180)
- binding pyrophosphate 2-: R113 (≠ V132), S131 (= S156), Q151 (≠ D176), T152 (= T177), G153 (= G178), G154 (= G179), S155 (= S180), R158 (≠ S183), P359 (= P397)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
32% identity, 89% coverage: 16:435/474 of query aligns to 10:397/412 of 1o9oA
- active site: K62 (= K81), A131 (≠ S156), S132 (= S157), T150 (≠ S175), T152 (= T177), G153 (= G178), G154 (= G179), S155 (= S180), R158 (≠ S183)
- binding 3-amino-3-oxopropanoic acid: G130 (= G155), T152 (= T177), G153 (= G178), G154 (= G179), S155 (= S180), R158 (≠ S183), P359 (= P397)
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
27% identity, 77% coverage: 73:437/474 of query aligns to 30:442/450 of 4n0iA
- active site: K38 (= K81), S116 (= S156), S117 (= S157), T135 (≠ S175), T137 (= T177), G138 (= G178), G139 (= G179), S140 (= S180), L143 (≠ S183)
- binding glutamine: G89 (vs. gap), T137 (= T177), G138 (= G178), S140 (= S180), Y168 (≠ L208), Y271 (≠ G306), Y272 (≠ A307), R320 (≠ N336), D404 (≠ P397)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
34% identity, 82% coverage: 51:440/474 of query aligns to 45:433/461 of 4gysB
- active site: K72 (= K81), S146 (= S156), S147 (= S157), T165 (≠ S175), T167 (= T177), A168 (≠ G178), G169 (= G179), S170 (= S180), V173 (≠ S183)
- binding malonate ion: A120 (= A130), G122 (= G133), S146 (= S156), T167 (= T177), A168 (≠ G178), S170 (= S180), S193 (≠ R203), G194 (= G204), V195 (= V205), R200 (≠ P210), Y297 (≠ I310), R305 (≠ A314)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
28% identity, 94% coverage: 14:457/474 of query aligns to 11:480/482 of 3a2qA
- active site: K69 (= K81), S147 (= S156), S148 (= S157), N166 (≠ S175), A168 (≠ T177), A169 (≠ G178), G170 (= G179), A171 (≠ S180), I174 (≠ S183)
- binding 6-aminohexanoic acid: G121 (≠ A130), G121 (≠ A130), N122 (≠ M131), S147 (= S156), A168 (≠ T177), A168 (≠ T177), A169 (≠ G178), A171 (≠ S180), C313 (≠ E292)
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)
40% identity, 30% coverage: 73:216/474 of query aligns to 28:173/425 of Q9FR37
- K36 (= K81) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S156) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S157) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D176) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S180) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C188) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 214 S→T: Slightly reduces catalytic activity.
Query Sequence
>WP_011969923.1 NCBI__GCF_000017145.1:WP_011969923.1
MIENPADLPILEAAERLRDGRLTSVALTVAHLDRIAERNGAYHAFLHVAAESALAEAARA
DEALGCGEDRGPLHGIPVAVKDLFDTAGMPTTYGSDVYAGYLPTEDAEVVRRLRAAGAVL
IGKLETYEFAMVGPVFDRSFPPAANPWDVRRFTGGSSSGSAAAVAGGLVRTSVASDTGGS
VRSPAAYCGVVGFKPTYGRIPARGVFVLSPSLDHVGLISASVAEAAITFDAIADAETTDA
EPAASRLGGALSGLRIGYARKWFADDPETLPALLDAVDGAASQLSLLGARIEEVALPAAP
DFESVGAVIIHAEAFEAHRRQLAASGDGYSRKVFQNILSGLCLTPEDLVRARHAAARLRD
RIDRTVFARFDAILTATTLTPAIPFADFAGEAARWTPMRTIAFNVTGHPALSVPCGFANG
LPLAIQLAGRAGDEATLCQIGHAYEQASDFAASKPPLPFPRAASDGRTQPAPSE
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