SitesBLAST
Comparing WP_012116033.1 NCBI__GCF_000017645.1:WP_012116033.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
33% identity, 96% coverage: 9:458/468 of query aligns to 7:477/490 of 4yjiA
- active site: K79 (= K81), S158 (= S156), S159 (= S157), G179 (= G177), G180 (= G178), G181 (= G179), A182 (≠ S180)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L83), G132 (= G130), S158 (= S156), G179 (= G177), G180 (= G178), A182 (≠ S180)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
32% identity, 82% coverage: 71:455/468 of query aligns to 85:498/508 of 3a1iA
- active site: K95 (= K81), S170 (= S156), S171 (= S157), G189 (≠ T175), Q191 (≠ G177), G192 (= G178), G193 (= G179), A194 (≠ S180), I197 (= I183)
- binding benzamide: F145 (≠ C131), S146 (≠ K132), G147 (≠ P133), Q191 (≠ G177), G192 (= G178), G193 (= G179), A194 (≠ S180), W327 (= W310)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 95% coverage: 13:455/468 of query aligns to 10:467/478 of 3h0mA
- active site: K72 (= K81), S147 (= S156), S148 (= S157), S166 (≠ T175), T168 (≠ G177), G169 (= G178), G170 (= G179), S171 (= S180), Q174 (≠ I183)
- binding glutamine: M122 (≠ C131), G123 (≠ K132), D167 (= D176), T168 (≠ G177), G169 (= G178), G170 (= G179), S171 (= S180), F199 (vs. gap), Y302 (≠ D308), R351 (≠ I340), D418 (≠ V405)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 95% coverage: 13:455/468 of query aligns to 10:467/478 of 3h0lA
- active site: K72 (= K81), S147 (= S156), S148 (= S157), S166 (≠ T175), T168 (≠ G177), G169 (= G178), G170 (= G179), S171 (= S180), Q174 (≠ I183)
- binding asparagine: G123 (≠ K132), S147 (= S156), G169 (= G178), G170 (= G179), S171 (= S180), Y302 (≠ D308), R351 (≠ I340), D418 (≠ V405)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
27% identity, 97% coverage: 1:454/468 of query aligns to 1:473/485 of 2f2aA
- active site: K79 (= K81), S154 (= S156), S155 (= S157), S173 (≠ T175), T175 (≠ G177), G176 (= G178), G177 (= G179), S178 (= S180), Q181 (≠ I183)
- binding glutamine: G130 (≠ K132), S154 (= S156), D174 (= D176), T175 (≠ G177), G176 (= G178), S178 (= S180), F206 (vs. gap), Y309 (vs. gap), Y310 (≠ Q300), R358 (vs. gap), D425 (≠ V405)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
27% identity, 97% coverage: 1:454/468 of query aligns to 1:473/485 of 2dqnA
- active site: K79 (= K81), S154 (= S156), S155 (= S157), S173 (≠ T175), T175 (≠ G177), G176 (= G178), G177 (= G179), S178 (= S180), Q181 (≠ I183)
- binding asparagine: M129 (≠ C131), G130 (≠ K132), T175 (≠ G177), G176 (= G178), S178 (= S180), Y309 (vs. gap), Y310 (≠ Q300), R358 (vs. gap), D425 (≠ V405)
3kfuE Crystal structure of the transamidosome (see paper)
32% identity, 97% coverage: 13:467/468 of query aligns to 5:467/468 of 3kfuE
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
29% identity, 88% coverage: 45:458/468 of query aligns to 168:592/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (= G130), T258 (≠ P133), S281 (= S156), G302 (= G177), G303 (= G178), S305 (= S180), S472 (≠ A338), I532 (≠ P393), M539 (≠ V402)
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, 88% coverage: 45:458/468 of query aligns to 168:592/607 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 (= GGGS 177:180) binding substrate
- S305 (= S180) mutation to A: Loss of activity.
- R307 (= R182) mutation to A: Loss of activity.
- S360 (≠ H234) mutation to A: No effect.
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
31% identity, 97% coverage: 4:458/468 of query aligns to 1:448/457 of 5h6sC
- active site: K77 (= K81), S152 (= S156), S153 (= S157), L173 (≠ G177), G174 (= G178), G175 (= G179), S176 (= S180)
- binding 4-oxidanylbenzohydrazide: C126 (≠ G130), R128 (≠ K132), W129 (≠ P133), S152 (= S156), L173 (≠ G177), G174 (= G178), S176 (= S180), W306 (≠ Y315), F338 (≠ L341)
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
28% identity, 88% coverage: 45:458/468 of query aligns to 168:592/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (= G130), G302 (= G177), G303 (= G178), G304 (= G179), A305 (≠ S180), V442 (= V301), I475 (≠ L341), M539 (≠ V402)
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
28% identity, 88% coverage: 45:458/468 of query aligns to 168:592/605 of 8ey1D
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
32% identity, 98% coverage: 8:464/468 of query aligns to 5:478/482 of 3a2qA
- active site: K69 (= K81), S147 (= S156), S148 (= S157), N166 (≠ T175), A168 (≠ G177), A169 (≠ G178), G170 (= G179), A171 (≠ S180), I174 (= I183)
- binding 6-aminohexanoic acid: G121 (= G130), G121 (= G130), N122 (≠ C131), S147 (= S156), A168 (≠ G177), A168 (≠ G177), A169 (≠ G178), A171 (≠ S180), C313 (≠ R323)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
29% identity, 96% coverage: 8:454/468 of query aligns to 1:448/457 of 6c6gA
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
36% identity, 49% coverage: 13:239/468 of query aligns to 11:244/487 of 1m21A
- active site: K81 (= K81), S160 (= S156), S161 (= S157), T179 (= T175), T181 (≠ G177), D182 (≠ G178), G183 (= G179), S184 (= S180), C187 (≠ I183)
- binding : A129 (vs. gap), N130 (vs. gap), F131 (vs. gap), C158 (≠ G154), G159 (= G155), S160 (= S156), S184 (= S180), C187 (≠ I183), I212 (≠ T205)
Sites not aligning to the query:
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
30% identity, 81% coverage: 73:453/468 of query aligns to 83:460/605 of Q936X2
- K91 (= K81) mutation to A: Loss of activity.
- S165 (= S156) mutation to A: Loss of activity.
- S189 (= S180) mutation to A: Loss of activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
29% identity, 88% coverage: 51:463/468 of query aligns to 45:447/461 of 4gysB
- active site: K72 (= K81), S146 (= S156), S147 (= S157), T165 (= T175), T167 (≠ G177), A168 (≠ G178), G169 (= G179), S170 (= S180), V173 (≠ I183)
- binding malonate ion: A120 (≠ G130), G122 (≠ K132), S146 (= S156), T167 (≠ G177), A168 (≠ G178), S170 (= S180), S193 (≠ V200), G194 (≠ P201), V195 (= V202), R200 (≠ P209), Y297 (vs. gap), R305 (≠ F314)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
28% identity, 91% coverage: 15:438/468 of query aligns to 35:471/507 of Q84DC4
- 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 (≠ I183) 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 (≠ D305) 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 (≠ S351) 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 (≠ V405) 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.
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)
35% identity, 49% coverage: 62:292/468 of query aligns to 122:357/579 of Q9TUI8
- S217 (= S156) mutation to A: Loss of activity.
- S218 (= S157) mutation to A: Lowers activity by at least 98%.
- D237 (= D176) mutation D->E,N: Loss of activity.
- S241 (= S180) mutation to A: Loss of activity.
- C249 (≠ S188) mutation to A: Loss of activity.
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
34% identity, 50% coverage: 4:235/468 of query aligns to 1:240/564 of 6te4A
Sites not aligning to the query:
Query Sequence
>WP_012116033.1 NCBI__GCF_000017645.1:WP_012116033.1
MSAEFDSMSALALRALVARREVSPVELTRRALDRAIATQPTLNAFFVIFEEEAMAAARVA
EDAVMAGAPLGLIHGLPFSAKDLMAVKGAPYASGSRAMADNIAEVDAPAVERAKAQGGIL
IGKTTTSEFGCKPIGDSPLTGITRNPWNLAMTPGGSSAGAAASVAAGITPFALGTDGGGS
IRIPCAFSGLSGLKGQFGRVPVWPTSATPTLAHVGPIARSMADAALLFSAVAGHDRRDPF
AVAGPVPDVMGAALASVAGLRVAYSPTFGYARPAPEVLAATDRAARTFEDLGCHVEQVEQ
VFDTDPADLWTAEFYAGVGTRLRDVLENRRELLDPAVADILMPALGQEMKSYYASVFARY
ALREKMRLFFERYDLLISPVLPVSALEAGRNLPEGLEDRNLVSWVFYTYPFNLTGQPAGA
VCAGLSPEGMPIGLQIVGRSHCEDDVVRAAAAFERAQPPGYNRPPVGA
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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