SitesBLAST
Comparing WP_068166836.1 NCBI__GCF_001592305.1:WP_068166836.1 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)
3kfuE Crystal structure of the transamidosome (see paper)
34% identity, 89% coverage: 8:458/504 of query aligns to 2:458/468 of 3kfuE
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
29% identity, 91% coverage: 1:459/504 of query aligns to 1:478/485 of 2f2aA
- active site: K79 (= K79), S154 (= S154), S155 (= S155), S173 (= S173), T175 (= T175), G176 (= G176), G177 (= G177), S178 (= S178), Q181 (≠ I181)
- binding glutamine: G130 (= G130), S154 (= S154), D174 (= D174), T175 (= T175), G176 (= G176), S178 (= S178), F206 (≠ G206), Y309 (≠ F307), Y310 (≠ D308), R358 (≠ N337), D425 (≠ L405)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
29% identity, 91% coverage: 1:459/504 of query aligns to 1:478/485 of 2dqnA
- active site: K79 (= K79), S154 (= S154), S155 (= S155), S173 (= S173), T175 (= T175), G176 (= G176), G177 (= G177), S178 (= S178), Q181 (≠ I181)
- binding asparagine: M129 (≠ A129), G130 (= G130), T175 (= T175), G176 (= G176), S178 (= S178), Y309 (≠ F307), Y310 (≠ D308), R358 (≠ N337), D425 (≠ L405)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 89% coverage: 7:457/504 of query aligns to 6:469/478 of 3h0mA
- active site: K72 (= K79), S147 (= S154), S148 (= S155), S166 (= S173), T168 (= T175), G169 (= G176), G170 (= G177), S171 (= S178), Q174 (≠ I181)
- binding glutamine: M122 (≠ A129), G123 (= G130), D167 (= D174), T168 (= T175), G169 (= G176), G170 (= G177), S171 (= S178), F199 (≠ G206), Y302 (vs. gap), R351 (≠ N337), D418 (≠ Y409)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 89% coverage: 7:457/504 of query aligns to 6:469/478 of 3h0lA
- active site: K72 (= K79), S147 (= S154), S148 (= S155), S166 (= S173), T168 (= T175), G169 (= G176), G170 (= G177), S171 (= S178), Q174 (≠ I181)
- binding asparagine: G123 (= G130), S147 (= S154), G169 (= G176), G170 (= G177), S171 (= S178), Y302 (vs. gap), R351 (≠ N337), D418 (≠ Y409)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
34% identity, 86% coverage: 6:438/504 of query aligns to 1:432/457 of 6c6gA
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
33% identity, 87% coverage: 19:457/504 of query aligns to 18:471/482 of 3a2qA
- active site: K69 (= K79), S147 (= S154), S148 (= S155), N166 (≠ S173), A168 (≠ T175), A169 (≠ G176), G170 (= G177), A171 (≠ S178), I174 (= I181)
- binding 6-aminohexanoic acid: G121 (= G128), G121 (= G128), N122 (≠ A129), S147 (= S154), A168 (≠ T175), A168 (≠ T175), A169 (≠ G176), A171 (≠ S178), C313 (vs. gap)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
28% identity, 90% coverage: 2:456/504 of query aligns to 1:475/490 of 4yjiA
- active site: K79 (= K79), S158 (= S154), S159 (= S155), G179 (≠ T175), G180 (= G176), G181 (= G177), A182 (≠ S178)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L81), G132 (= G128), S158 (= S154), G179 (≠ T175), G180 (= G176), A182 (≠ S178)
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
25% identity, 87% coverage: 17:454/504 of query aligns to 140:588/607 of Q7XJJ7
- K205 (= K79) mutation to A: Loss of activity.
- SS 281:282 (= SS 154:155) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 175:178) binding substrate
- S305 (= S178) mutation to A: Loss of activity.
- R307 (= R180) mutation to A: Loss of activity.
- S360 (≠ R233) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
25% identity, 87% coverage: 17:454/504 of query aligns to 140:588/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (= G128), T258 (≠ A131), S281 (= S154), G302 (≠ T175), G303 (= G176), S305 (= S178), S472 (≠ N337), I532 (≠ L405), M539 (≠ Y409)
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
24% identity, 87% coverage: 17:454/504 of query aligns to 140:588/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (= G128), G302 (≠ T175), G303 (= G176), G304 (= G177), A305 (≠ S178), V442 (≠ F315), I475 (≠ M340), M539 (≠ Y409)
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
24% identity, 87% coverage: 17:454/504 of query aligns to 140:588/605 of 8ey1D
8xtcA umgsp2-mut (see paper)
33% identity, 87% coverage: 2:437/504 of query aligns to 1:418/440 of 8xtcA
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
28% identity, 87% coverage: 6:445/504 of query aligns to 5:445/457 of 5h6sC
- active site: K77 (= K79), S152 (= S154), S153 (= S155), L173 (≠ T175), G174 (= G176), G175 (= G177), S176 (= S178)
- binding 4-oxidanylbenzohydrazide: C126 (≠ G128), R128 (≠ G130), W129 (≠ A131), S152 (= S154), L173 (≠ T175), G174 (= G176), S176 (= S178), W306 (≠ L310), F338 (≠ A341)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
31% identity, 78% coverage: 69:462/504 of query aligns to 85:508/508 of 3a1iA
- active site: K95 (= K79), S170 (= S154), S171 (= S155), G189 (≠ S173), Q191 (≠ T175), G192 (= G176), G193 (= G177), A194 (≠ S178), I197 (= I181)
- binding benzamide: F145 (≠ A129), S146 (≠ G130), G147 (≠ A131), Q191 (≠ T175), G192 (= G176), G193 (= G177), A194 (≠ S178), W327 (vs. gap)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
29% identity, 90% coverage: 6:458/504 of query aligns to 2:411/412 of 1o9oA
- active site: K62 (= K79), A131 (≠ S154), S132 (= S155), T150 (≠ S173), T152 (= T175), G153 (= G176), G154 (= G177), S155 (= S178), R158 (≠ I181)
- binding 3-amino-3-oxopropanoic acid: G130 (= G153), T152 (= T175), G153 (= G176), G154 (= G177), S155 (= S178), R158 (≠ I181), P359 (≠ G395)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
29% identity, 90% coverage: 6:458/504 of query aligns to 2:411/412 of 1ocmA
- active site: K62 (= K79), S131 (= S154), S132 (= S155), T152 (= T175), G153 (= G176), G154 (= G177), S155 (= S178)
- binding pyrophosphate 2-: R113 (= R134), S131 (= S154), Q151 (≠ D174), T152 (= T175), G153 (= G176), G154 (= G177), S155 (= S178), R158 (≠ I181), P359 (≠ G395)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
35% identity, 46% coverage: 10:242/504 of query aligns to 10:248/487 of 1m21A
- active site: K81 (= K79), S160 (= S154), S161 (= S155), T179 (≠ S173), T181 (= T175), D182 (≠ G176), G183 (= G177), S184 (= S178), C187 (≠ I181)
- binding : A129 (= A131), N130 (= N132), F131 (≠ T133), C158 (≠ G152), G159 (= G153), S160 (= S154), S184 (= S178), C187 (≠ I181), I212 (≠ L205)
Sites not aligning to the query:
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
28% identity, 80% coverage: 49:453/504 of query aligns to 62:460/605 of Q936X2
- K91 (= K79) mutation to A: Loss of activity.
- S165 (= S154) mutation to A: Loss of activity.
- S189 (= S178) mutation to A: Loss of activity.
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
30% identity, 90% coverage: 1:455/504 of query aligns to 28:488/507 of Q84DC4
- T31 (≠ V4) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K79) mutation to A: Abolishes activity on mandelamide.
- S180 (= S154) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S155) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G176) 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 (= S178) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ I181) 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 (≠ R282) 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 (≠ M340) 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 (≠ T408) 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.
Query Sequence
>WP_068166836.1 NCBI__GCF_001592305.1:WP_068166836.1
MSLVHLSAVELRRRIGNKEISPVELLEACIARIEAVNPAVNAICATDHERARAAARTAEA
QVLRGEALGALHGLPLGVKDLQDTAGLLTTSGNVGRRGNVPQQDNALVARLRAAGAIVTA
KTNVPDMGAGANTRNPVWGATGNPFNPLLNAGGSSGGSAAALATDMLPLCTGSDTGGSLR
IPAALCGVVGLRPSPGVVANDARPLGWSVISVLGPMGRTVADTALMLSASVGRHPMDPLS
VSGVCQGWPVRELDLASLRIGTVEDFGACAVDPSIRRTFRQRVAALARHTRSCEPLDLSL
PDGHRCFDILRAESFVAAFADTYRQDPQSLGPNVRANVEMAHAITLGDRAWAHLEQTRIA
RRFERAFEQVDLIVAPVTPISPFPWSELYAECIDGQAMRNYYEWLGLTYMVTLATNPALS
LPCGVDEQGMPFGLQLIAPLRADDRLLAMASAIEAAFAMDAELCRPRPPEAVLAQAQPTL
KSLVTHPPLLERAAPATAASDTAV
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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