SitesBLAST
Comparing WP_012115219.1 NCBI__GCF_000017645.1:WP_012115219.1 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)
30% identity, 95% coverage: 16:463/474 of query aligns to 15:479/485 of 2f2aA
- active site: K79 (= K80), S154 (= S155), S155 (= S156), S173 (= S174), T175 (= T176), G176 (= G177), G177 (= G178), S178 (= S179), Q181 (≠ H182)
- binding glutamine: G130 (≠ S131), S154 (= S155), D174 (= D175), T175 (= T176), G176 (= G177), S178 (= S179), F206 (≠ L207), Y309 (≠ M310), Y310 (≠ Q311), R358 (= R340), D425 (≠ R406)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
30% identity, 95% coverage: 16:463/474 of query aligns to 15:479/485 of 2dqnA
- active site: K79 (= K80), S154 (= S155), S155 (= S156), S173 (= S174), T175 (= T176), G176 (= G177), G177 (= G178), S178 (= S179), Q181 (≠ H182)
- binding asparagine: M129 (≠ L130), G130 (≠ S131), T175 (= T176), G176 (= G177), S178 (= S179), Y309 (≠ M310), Y310 (≠ Q311), R358 (= R340), D425 (≠ R406)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
35% identity, 95% coverage: 7:457/474 of query aligns to 1:448/457 of 6c6gA
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 96% coverage: 11:467/474 of query aligns to 9:476/478 of 3h0mA
- active site: K72 (= K80), S147 (= S155), S148 (= S156), S166 (= S174), T168 (= T176), G169 (= G177), G170 (= G178), S171 (= S179), Q174 (≠ H182)
- binding glutamine: M122 (≠ L130), G123 (vs. gap), D167 (= D175), T168 (= T176), G169 (= G177), G170 (= G178), S171 (= S179), F199 (≠ L207), Y302 (vs. gap), R351 (= R340), D418 (= D399)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 96% coverage: 11:467/474 of query aligns to 9:476/478 of 3h0lA
- active site: K72 (= K80), S147 (= S155), S148 (= S156), S166 (= S174), T168 (= T176), G169 (= G177), G170 (= G178), S171 (= S179), Q174 (≠ H182)
- binding asparagine: G123 (vs. gap), S147 (= S155), G169 (= G177), G170 (= G178), S171 (= S179), Y302 (vs. gap), R351 (= R340), D418 (= D399)
3kfuE Crystal structure of the transamidosome (see paper)
35% identity, 95% coverage: 11:460/474 of query aligns to 4:457/468 of 3kfuE
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
32% identity, 95% coverage: 9:460/474 of query aligns to 8:479/487 of 1m21A
- active site: K81 (= K80), S160 (= S155), S161 (= S156), T179 (≠ S174), T181 (= T176), D182 (≠ G177), G183 (= G178), S184 (= S179), C187 (≠ H182)
- binding : A129 (= A129), N130 (≠ L130), F131 (vs. gap), C158 (≠ G153), G159 (= G154), S160 (= S155), S184 (= S179), C187 (≠ H182), I212 (≠ L207), R318 (≠ Q311), L321 (≠ M314), L365 (vs. gap), F426 (≠ G395)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
28% identity, 81% coverage: 65:450/474 of query aligns to 190:581/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A129), T258 (≠ P132), S281 (= S155), G302 (≠ T176), G303 (= G177), S305 (= S179), S472 (≠ R340), I532 (≠ A401), M539 (≠ A408)
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)
27% identity, 86% coverage: 44:450/474 of query aligns to 169:581/607 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 (≠ TGGS 176:179) binding
- S305 (= S179) mutation to A: Loss of activity.
- R307 (= R181) mutation to A: Loss of activity.
- S360 (≠ P234) mutation to A: No effect.
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
32% identity, 82% coverage: 70:458/474 of query aligns to 85:498/508 of 3a1iA
- active site: K95 (= K80), S170 (= S155), S171 (= S156), G189 (≠ S174), Q191 (≠ T176), G192 (= G177), G193 (= G178), A194 (≠ S179), I197 (≠ H182)
- binding benzamide: F145 (≠ L130), S146 (= S131), G147 (≠ P132), Q191 (≠ T176), G192 (= G177), G193 (= G178), A194 (≠ S179), W327 (≠ M310)
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)
27% identity, 81% coverage: 72:455/474 of query aligns to 28:420/425 of Q9FR37
- K36 (= K80) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S155) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S156) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D175) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S179) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C187) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (≠ T241) mutation to T: Slightly reduces catalytic activity.
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
28% identity, 96% coverage: 7:459/474 of query aligns to 5:446/457 of 5h6sC
- active site: K77 (= K80), S152 (= S155), S153 (= S156), L173 (≠ T176), G174 (= G177), G175 (= G178), S176 (= S179)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A129), R128 (≠ S131), W129 (≠ P132), S152 (= S155), L173 (≠ T176), G174 (= G177), S176 (= S179), W306 (= W325), F338 (vs. gap)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
28% identity, 95% coverage: 4:454/474 of query aligns to 25:484/507 of Q84DC4
- T31 (≠ V10) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- 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 (= G177) 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 (≠ H182) 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 (≠ V306) 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 (≠ R351) 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 (= I414) 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.
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
29% identity, 95% coverage: 11:458/474 of query aligns to 10:474/490 of 4yjiA
- active site: K79 (= K80), S158 (= S155), S159 (= S156), G179 (≠ T176), G180 (= G177), G181 (= G178), A182 (≠ S179)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L82), G132 (≠ A129), S158 (= S155), G179 (≠ T176), G180 (= G177), A182 (≠ S179)
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
33% identity, 49% coverage: 7:236/474 of query aligns to 5:241/564 of 6te4A
Sites not aligning to the query:
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
29% identity, 93% coverage: 12:451/474 of query aligns to 10:462/482 of 3a2qA
- active site: K69 (= K80), S147 (= S155), S148 (= S156), N166 (≠ S174), A168 (≠ T176), A169 (≠ G177), G170 (= G178), A171 (≠ S179), I174 (≠ H182)
- binding 6-aminohexanoic acid: G121 (≠ A129), G121 (≠ A129), N122 (≠ L130), S147 (= S155), A168 (≠ T176), A168 (≠ T176), A169 (≠ G177), A171 (≠ S179), C313 (≠ V313)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
29% identity, 83% coverage: 63:456/474 of query aligns to 75:460/605 of Q936X2
- K91 (= K80) mutation to A: Loss of activity.
- S165 (= S155) mutation to A: Loss of activity.
- S189 (= S179) mutation to A: Loss of activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
28% identity, 95% coverage: 24:471/474 of query aligns to 19:446/461 of 4gysB
- active site: K72 (= K80), S146 (= S155), S147 (= S156), T165 (≠ S174), T167 (= T176), A168 (≠ G177), G169 (= G178), S170 (= S179), V173 (≠ H182)
- binding malonate ion: A120 (= A129), G122 (≠ S131), S146 (= S155), T167 (= T176), A168 (≠ G177), S170 (= S179), S193 (≠ Y202), G194 (= G203), V195 (≠ A204), R200 (≠ P209), Y297 (≠ Q311), R305 (≠ L315)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
27% identity, 80% coverage: 64:442/474 of query aligns to 46:392/412 of 1ocmA
- active site: K62 (= K80), S131 (= S155), S132 (= S156), T152 (= T176), G153 (= G177), G154 (= G178), S155 (= S179)
- binding pyrophosphate 2-: R113 (≠ L130), S131 (= S155), Q151 (≠ D175), T152 (= T176), G153 (= G177), G154 (= G178), S155 (= S179), R158 (≠ H182), P359 (= P397)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
27% identity, 80% coverage: 64:442/474 of query aligns to 46:392/412 of 1o9oA
- active site: K62 (= K80), A131 (≠ S155), S132 (= S156), T150 (≠ S174), T152 (= T176), G153 (= G177), G154 (= G178), S155 (= S179), R158 (≠ H182)
- binding 3-amino-3-oxopropanoic acid: G130 (= G154), T152 (= T176), G153 (= G177), G154 (= G178), S155 (= S179), R158 (≠ H182), P359 (= P397)
Query Sequence
>WP_012115219.1 NCBI__GCF_000017645.1:WP_012115219.1
MSGFFTLGVVEMADAVADGSVSSEALAEEALQRLETLGPRYNAVMQIEPERAREAARAVD
LARARGDKLGPLAGVPLAHKDLLYRAGRVATGGSLIRKDFVPDVTSSVLERLDAAGALDL
GSLHLAEFALSPTGFNVHYGHGLSPWNTAYGAGGSSSGSGAAVAARMVPGALGSDTGGSI
RHPSAMCGVTGLKPTHGLVPLYGAMPLAPSLDTIGPLTRTARDAARMMTAIAGPDPRDGA
TLPAPRLDFEGGLKGDLKGLTIAVPSGYYRELATPEIAALMDDSRAVLKDAGAQLIETSP
PDMALVNALMQVVMLVEMSTLHRRWLTERPQDYSLQVRARMLPGLALPATRYAEALMMRA
SVTRDWLATTMGAADMVHMPTLPVAVPSIAETTAGPPEDIAAVVGRLAAFTRGINYLGLP
SLSVPCGFTANGLPAAFQLVGRPYADPVLLKAGDAYQRRTDFHALLPPGCGALA
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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