SitesBLAST
Comparing WP_011973717.1 NCBI__GCF_000017185.1:WP_011973717.1 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)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
43% identity, 92% coverage: 35:434/434 of query aligns to 49:469/478 of 3h0mA
- active site: K72 (= K56), S147 (= S131), S148 (= S132), S166 (= S150), T168 (= T152), G169 (= G153), G170 (= G154), S171 (= S155), Q174 (≠ N158)
- binding glutamine: M122 (≠ S106), G123 (= G107), D167 (= D151), T168 (= T152), G169 (= G153), G170 (= G154), S171 (= S155), F199 (≠ L183), Y302 (= Y282), R351 (= R317), D418 (= D383)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
43% identity, 92% coverage: 35:434/434 of query aligns to 49:469/478 of 3h0lA
- active site: K72 (= K56), S147 (= S131), S148 (= S132), S166 (= S150), T168 (= T152), G169 (= G153), G170 (= G154), S171 (= S155), Q174 (≠ N158)
- binding asparagine: G123 (= G107), S147 (= S131), G169 (= G153), G170 (= G154), S171 (= S155), Y302 (= Y282), R351 (= R317), D418 (= D383)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
39% identity, 97% coverage: 12:434/434 of query aligns to 31:476/485 of 2f2aA
- active site: K79 (= K56), S154 (= S131), S155 (= S132), S173 (= S150), T175 (= T152), G176 (= G153), G177 (= G154), S178 (= S155), Q181 (≠ N158)
- binding glutamine: G130 (= G107), S154 (= S131), D174 (= D151), T175 (= T152), G176 (= G153), S178 (= S155), F206 (≠ L183), Y309 (= Y282), Y310 (= Y283), R358 (= R317), D425 (= D383)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
39% identity, 97% coverage: 12:434/434 of query aligns to 31:476/485 of 2dqnA
- active site: K79 (= K56), S154 (= S131), S155 (= S132), S173 (= S150), T175 (= T152), G176 (= G153), G177 (= G154), S178 (= S155), Q181 (≠ N158)
- binding asparagine: M129 (≠ S106), G130 (= G107), T175 (= T152), G176 (= G153), S178 (= S155), Y309 (= Y282), Y310 (= Y283), R358 (= R317), D425 (= D383)
3kfuE Crystal structure of the transamidosome (see paper)
36% identity, 100% coverage: 1:432/434 of query aligns to 14:455/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
34% identity, 87% coverage: 48:425/434 of query aligns to 30:444/450 of 4n0iA
- active site: K38 (= K56), S116 (= S131), S117 (= S132), T135 (≠ S150), T137 (= T152), G138 (= G153), G139 (= G154), S140 (= S155), L143 (≠ N158)
- binding glutamine: G89 (= G107), T137 (= T152), G138 (= G153), S140 (= S155), Y168 (≠ L183), Y271 (= Y282), Y272 (= Y283), R320 (= R317), D404 (= D383)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
29% identity, 89% coverage: 48:432/434 of query aligns to 87:498/508 of 3a1iA
- active site: K95 (= K56), S170 (= S131), S171 (= S132), G189 (≠ S150), Q191 (≠ T152), G192 (= G153), G193 (= G154), A194 (≠ S155), I197 (≠ N158)
- binding benzamide: F145 (≠ S106), S146 (≠ G107), G147 (≠ S108), Q191 (≠ T152), G192 (= G153), G193 (= G154), A194 (≠ S155), W327 (≠ I285)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
29% identity, 95% coverage: 22:432/434 of query aligns to 169:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A105), T258 (≠ S108), S281 (= S131), G302 (≠ T152), G303 (= G153), S305 (= S155), S472 (≠ G311), I532 (≠ E378), M539 (≠ L385)
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, 95% coverage: 22:432/434 of query aligns to 169:589/607 of Q7XJJ7
- K205 (= K56) mutation to A: Loss of activity.
- SS 281:282 (= SS 131:132) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 152:155) binding
- S305 (= S155) mutation to A: Loss of activity.
- R307 (= R157) mutation to A: Loss of activity.
- S360 (≠ K210) mutation to A: No effect.
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
27% identity, 94% coverage: 19:426/434 of query aligns to 35:443/457 of 6c6gA
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
25% identity, 98% coverage: 10:433/434 of query aligns to 29:478/487 of 1m21A
- active site: K81 (= K56), S160 (= S131), S161 (= S132), T179 (≠ S150), T181 (= T152), D182 (≠ G153), G183 (= G154), S184 (= S155), C187 (≠ N158)
- binding : A129 (= A105), N130 (≠ S106), F131 (vs. gap), C158 (≠ G129), G159 (= G130), S160 (= S131), S184 (= S155), C187 (≠ N158), I212 (≠ L183), R318 (≠ L277), L321 (≠ P280), L365 (≠ I318), F426 (≠ T375)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
26% identity, 96% coverage: 10:425/434 of query aligns to 51:481/507 of Q84DC4
- K100 (= K56) mutation to A: Abolishes activity on mandelamide.
- S180 (= S131) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S132) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G153) 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 (= S155) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ N158) 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 (≠ A278) 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 (≠ K336) 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 (≠ V384) 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.
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)
44% identity, 34% coverage: 48:195/434 of query aligns to 28:177/425 of Q9FR37
- K36 (= K56) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S131) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S132) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D151) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S155) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C163) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 214 S→T: Slightly reduces catalytic activity.
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
24% identity, 98% coverage: 9:433/434 of query aligns to 27:446/457 of 5h6sC
- active site: K77 (= K56), S152 (= S131), S153 (= S132), L173 (≠ T152), G174 (= G153), G175 (= G154), S176 (= S155)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A105), R128 (≠ G107), W129 (≠ S108), S152 (= S131), L173 (≠ T152), G174 (= G153), S176 (= S155), W306 (≠ F291), F338 (≠ S330)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
29% identity, 91% coverage: 27:423/434 of query aligns to 44:430/461 of 4gysB
- active site: K72 (= K56), S146 (= S131), S147 (= S132), T165 (≠ S150), T167 (= T152), A168 (≠ G153), G169 (= G154), S170 (= S155), V173 (≠ N158)
- binding malonate ion: A120 (= A105), G122 (= G107), S146 (= S131), T167 (= T152), A168 (≠ G153), S170 (= S155), S193 (≠ Q178), G194 (= G179), V195 (≠ L180), R200 (≠ M185), Y297 (= Y282), R305 (≠ F290)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
27% identity, 89% coverage: 37:423/434 of query aligns to 68:453/605 of Q936X2
- K91 (= K56) mutation to A: Loss of activity.
- S165 (= S131) mutation to A: Loss of activity.
- S189 (= S155) mutation to A: Loss of activity.
Q9MUK5 Translocon at the outer membrane of chloroplasts 64 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
46% identity, 24% coverage: 92:195/434 of query aligns to 107:210/593 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.
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
25% identity, 97% coverage: 11:432/434 of query aligns to 30:474/490 of 4yjiA
- active site: K79 (≠ Y64), S158 (= S131), S159 (= S132), G179 (≠ T152), G180 (= G153), G181 (= G154), A182 (≠ S155)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ I66), G132 (≠ A105), S158 (= S131), G179 (≠ T152), G180 (= G153), A182 (≠ S155)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
24% identity, 95% coverage: 12:424/434 of query aligns to 9:400/412 of 1o9oA
- active site: K62 (= K56), A131 (≠ S131), S132 (= S132), T150 (≠ S150), T152 (= T152), G153 (= G153), G154 (= G154), S155 (= S155), R158 (≠ N158)
- binding 3-amino-3-oxopropanoic acid: G130 (= G130), T152 (= T152), G153 (= G153), G154 (= G154), S155 (= S155), R158 (≠ N158), P359 (≠ Y380)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
24% identity, 95% coverage: 12:424/434 of query aligns to 9:400/412 of 1ocmA
- active site: K62 (= K56), S131 (= S131), S132 (= S132), T152 (= T152), G153 (= G153), G154 (= G154), S155 (= S155)
- binding pyrophosphate 2-: R113 (≠ G107), S131 (= S131), Q151 (≠ D151), T152 (= T152), G153 (= G153), G154 (= G154), S155 (= S155), R158 (≠ N158), P359 (≠ Y380)
Query Sequence
>WP_011973717.1 NCBI__GCF_000017185.1:WP_011973717.1
MTIIDKALKYIEKIEKSDINAIIQLDKEKVLNEAKELENNEKLKNKPLYGKIIAIKSNIN
VKGYNISCASKTLENYISAYDATVVKKIKSQGGLIIGMTNMDEFASGSSGETSYYGATKN
PNAEGKIPGGSSSGSASAVAGDLCDMALGSDTGGSIRNPASHCGVVGFKPSYGVVSRQGL
CDLAMSFDQIGPLTKSAEDALLLTNIIKGKDLSDSTTVETPKFEKNEKQVKKYKVGIVKE
FMEVSDEKIRNKIEEGIEVFKDMGCKIVELNYKYTDLALPTYYLINYVEFFSATRKYDGR
RYGYPIEEVCGEEVLRRILIGKHISEQEFSGKYYKKALYTRKLMKNEMLKLFNDVDIIVS
PTVPKLPHNIGKELTPMEMYSYDVLTVPTNICGICAGVVKCGNIAGNPVGLQIQGKPFDD
EKVLNAMIEFEKQY
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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