SitesBLAST
Comparing WP_012332965.1 NCBI__GCF_000019365.1:WP_012332965.1 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)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
36% identity, 94% coverage: 21:459/469 of query aligns to 20:478/490 of 4yjiA
- active site: K79 (= K80), S158 (= S155), S159 (= S156), G179 (= G176), G180 (≠ A177), G181 (= G178), A182 (≠ S179)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ N82), G132 (= G129), S158 (= S155), G179 (= G176), G180 (≠ A177), A182 (≠ S179)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
33% identity, 99% coverage: 3:468/469 of query aligns to 1:456/457 of 5h6sC
- active site: K77 (= K80), S152 (= S155), S153 (= S156), L173 (≠ G176), G174 (≠ A177), G175 (= G178), S176 (= S179)
- binding 4-oxidanylbenzohydrazide: C126 (≠ G129), R128 (≠ K131), W129 (≠ G132), S152 (= S155), L173 (≠ G176), G174 (≠ A177), S176 (= S179), W306 (= W313), F338 (≠ R337)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
37% identity, 84% coverage: 67:461/469 of query aligns to 82:507/508 of 3a1iA
- active site: K95 (= K80), S170 (= S155), S171 (= S156), G189 (≠ T174), Q191 (≠ G176), G192 (≠ A177), G193 (= G178), A194 (≠ S179), I197 (= I182)
- binding benzamide: F145 (≠ W130), S146 (≠ K131), G147 (= G132), Q191 (≠ G176), G192 (≠ A177), G193 (= G178), A194 (≠ S179), W327 (≠ L309)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
29% identity, 96% coverage: 4:455/469 of query aligns to 3:474/485 of 2f2aA
- active site: K79 (= K80), S154 (= S155), S155 (= S156), S173 (≠ T174), T175 (≠ G176), G176 (≠ A177), G177 (= G178), S178 (= S179), Q181 (≠ I182)
- binding glutamine: G130 (≠ K131), S154 (= S155), D174 (= D175), T175 (≠ G176), G176 (≠ A177), S178 (= S179), F206 (vs. gap), Y309 (vs. gap), Y310 (vs. gap), R358 (vs. gap), D425 (≠ T405)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
29% identity, 96% coverage: 4:455/469 of query aligns to 3:474/485 of 2dqnA
- active site: K79 (= K80), S154 (= S155), S155 (= S156), S173 (≠ T174), T175 (≠ G176), G176 (≠ A177), G177 (= G178), S178 (= S179), Q181 (≠ I182)
- binding asparagine: M129 (≠ W130), G130 (≠ K131), T175 (≠ G176), G176 (≠ A177), S178 (= S179), Y309 (vs. gap), Y310 (vs. gap), R358 (vs. gap), D425 (≠ T405)
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
32% identity, 88% coverage: 44:458/469 of query aligns to 169:592/607 of Q7XJJ7
- K205 (= K80) mutation to A: Loss of activity.
- SS 281:282 (= SS 155:156) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ GAGS 176:179) binding substrate
- S305 (= S179) mutation to A: Loss of activity.
- R307 (= R181) mutation to A: Loss of activity.
- S360 (≠ P233) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
32% identity, 88% coverage: 44:458/469 of query aligns to 169:592/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (= G129), T258 (≠ G132), S281 (= S155), G302 (= G176), G303 (≠ A177), S305 (= S179), S472 (≠ A339), I532 (≠ L402), M539 (vs. gap)
Sites not aligning to the query:
3kfuE Crystal structure of the transamidosome (see paper)
35% identity, 97% coverage: 12:465/469 of query aligns to 5:465/468 of 3kfuE
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
32% identity, 88% coverage: 44:458/469 of query aligns to 169:592/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (= G129), G302 (= G176), G303 (≠ A177), G304 (= G178), A305 (≠ S179), V442 (≠ I312), I475 (≠ R342), M539 (vs. gap)
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
32% identity, 88% coverage: 44:458/469 of query aligns to 169:592/605 of 8ey1D
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
30% identity, 97% coverage: 8:461/469 of query aligns to 6:475/482 of 3a2qA
- active site: K69 (= K80), S147 (= S155), S148 (= S156), N166 (≠ T174), A168 (≠ G176), A169 (= A177), G170 (= G178), A171 (≠ S179), I174 (= I182)
- binding 6-aminohexanoic acid: G121 (= G129), G121 (= G129), N122 (≠ W130), S147 (= S155), A168 (≠ G176), A168 (≠ G176), A169 (= A177), A171 (≠ S179), C313 (≠ G316)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 93% coverage: 19:454/469 of query aligns to 17:466/478 of 3h0mA
- active site: K72 (= K80), S147 (= S155), S148 (= S156), S166 (≠ T174), T168 (≠ G176), G169 (≠ A177), G170 (= G178), S171 (= S179), Q174 (≠ I182)
- binding glutamine: M122 (≠ W130), G123 (≠ K131), D167 (= D175), T168 (≠ G176), G169 (≠ A177), G170 (= G178), S171 (= S179), F199 (= F207), Y302 (≠ L309), R351 (vs. gap), D418 (= D399)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 93% coverage: 19:454/469 of query aligns to 17:466/478 of 3h0lA
- active site: K72 (= K80), S147 (= S155), S148 (= S156), S166 (≠ T174), T168 (≠ G176), G169 (≠ A177), G170 (= G178), S171 (= S179), Q174 (≠ I182)
- binding asparagine: G123 (≠ K131), S147 (= S155), G169 (≠ A177), G170 (= G178), S171 (= S179), Y302 (≠ L309), R351 (vs. gap), D418 (= D399)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
40% identity, 52% coverage: 19:261/469 of query aligns to 13:257/457 of 6c6gA
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
31% identity, 93% coverage: 21:455/469 of query aligns to 42:488/507 of Q84DC4
- K100 (= K80) mutation to A: Abolishes activity on mandelamide.
- S180 (= S155) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S156) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ A177) 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 (= S179) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ I182) 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 (≠ A270) 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 (≠ P334) 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 (≠ T405) 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.
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
28% identity, 91% coverage: 25:453/469 of query aligns to 37:460/605 of Q936X2
- K91 (= K80) mutation to A: Loss of activity.
- S165 (≠ A162) mutation to A: Loss of activity.
- S189 (= S179) mutation to A: Loss of activity.
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
32% identity, 95% coverage: 8:454/469 of query aligns to 7:476/487 of 1m21A
- active site: K81 (= K80), S160 (= S155), S161 (= S156), T179 (= T174), T181 (≠ G176), D182 (≠ A177), G183 (= G178), S184 (= S179), C187 (≠ I182)
- binding : A129 (vs. gap), N130 (vs. gap), F131 (vs. gap), C158 (≠ G153), G159 (= G154), S160 (= S155), S184 (= S179), C187 (≠ I182), I212 (≠ F207), R318 (= R329), L321 (≠ V332), L365 (vs. gap), F426 (≠ W401)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
31% identity, 83% coverage: 71:458/469 of query aligns to 63:443/461 of 4gysB
- active site: K72 (= K80), S146 (= S155), S147 (= S156), T165 (= T174), T167 (≠ G176), A168 (= A177), G169 (= G178), S170 (= S179), V173 (≠ I182)
- binding malonate ion: A120 (≠ G129), G122 (≠ K131), S146 (= S155), T167 (≠ G176), A168 (= A177), S170 (= S179), S193 (≠ Y202), G194 (≠ P203), V195 (≠ P204), R200 (vs. gap), Y297 (≠ N310), R305 (= R322)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
28% identity, 95% coverage: 10:456/469 of query aligns to 5:409/412 of 1o9oA
- active site: K62 (= K80), A131 (≠ S155), S132 (= S156), T150 (= T174), T152 (≠ G176), G153 (≠ A177), G154 (= G178), S155 (= S179), R158 (≠ I182)
- binding 3-amino-3-oxopropanoic acid: G130 (= G154), T152 (≠ G176), G153 (≠ A177), G154 (= G178), S155 (= S179), R158 (≠ I182), P359 (≠ T405)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
28% identity, 95% coverage: 10:456/469 of query aligns to 5:409/412 of 1ocmA
- active site: K62 (= K80), S131 (= S155), S132 (= S156), T152 (≠ G176), G153 (≠ A177), G154 (= G178), S155 (= S179)
- binding pyrophosphate 2-: R113 (≠ K131), S131 (= S155), Q151 (≠ D175), T152 (≠ G176), G153 (≠ A177), G154 (= G178), S155 (= S179), R158 (≠ I182), P359 (≠ T405)
Query Sequence
>WP_012332965.1 NCBI__GCF_000019365.1:WP_012332965.1
MTEIRHLDGAALAARYSDGALSPREVVADSLARIAAHEPAINAFVLVDAEAALARAAESE
ARWRAGTPRGPLDGIPVTIKDNIAWAGHPMRRGSPTTSPEPLAASAPATERLLEAGAIPL
GKTTMPEFGWKGLGDSTLTGPTRNPWDLSRTTGGSSAGAAAAAALDLGLAHLGTDGAGSI
RIPAAFCGVFGLKPSYGRVPAYPPSPFGPVAHLGPLARRVSDAALMLRAIARPDARDMLA
WLSEPPDYAAGLAAGVRGLRIAWSPRLGYAARVDPEVEALTARAASAFAELGATVEEADP
GFADPVETLNGIWLVGAWSVLRTIPEAQRGAVEPALRAAAERGSRISAPDFLAALNARAA
IFTAMARFHARYDLLLTPAVAVPALPVGRLTPADGSEGDDWLAWTPFSYPFNLTGQPAAS
VPCGLSAAGLPVGLQIVGPMGEDARVLAAARAFEAARPWPAIEAPRPAP
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