SitesBLAST
Comparing WP_015798951.1 NCBI__GCF_000023265.1:WP_015798951.1 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)
50% identity, 96% coverage: 13:474/479 of query aligns to 9:466/478 of 3h0mA
- active site: K72 (= K82), S147 (= S157), S148 (= S158), S166 (= S176), T168 (= T178), G169 (= G179), G170 (= G180), S171 (= S181), Q174 (= Q184)
- binding glutamine: M122 (= M132), G123 (= G133), D167 (= D177), T168 (= T178), G169 (= G179), G170 (= G180), S171 (= S181), F199 (= F209), Y302 (= Y310), R351 (= R358), D418 (= D425)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
50% identity, 96% coverage: 13:474/479 of query aligns to 9:466/478 of 3h0lA
- active site: K72 (= K82), S147 (= S157), S148 (= S158), S166 (= S176), T168 (= T178), G169 (= G179), G170 (= G180), S171 (= S181), Q174 (= Q184)
- binding asparagine: G123 (= G133), S147 (= S157), G169 (= G179), G170 (= G180), S171 (= S181), Y302 (= Y310), R351 (= R358), D418 (= D425)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
45% identity, 97% coverage: 13:475/479 of query aligns to 10:474/485 of 2f2aA
- active site: K79 (= K82), S154 (= S157), S155 (= S158), S173 (= S176), T175 (= T178), G176 (= G179), G177 (= G180), S178 (= S181), Q181 (= Q184)
- binding glutamine: G130 (= G133), S154 (= S157), D174 (= D177), T175 (= T178), G176 (= G179), S178 (= S181), F206 (= F209), Y309 (= Y310), Y310 (= Y311), R358 (= R358), D425 (= D425)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
45% identity, 97% coverage: 13:475/479 of query aligns to 10:474/485 of 2dqnA
- active site: K79 (= K82), S154 (= S157), S155 (= S158), S173 (= S176), T175 (= T178), G176 (= G179), G177 (= G180), S178 (= S181), Q181 (= Q184)
- binding asparagine: M129 (= M132), G130 (= G133), T175 (= T178), G176 (= G179), S178 (= S181), Y309 (= Y310), Y310 (= Y311), R358 (= R358), D425 (= D425)
3kfuE Crystal structure of the transamidosome (see paper)
52% identity, 98% coverage: 11:479/479 of query aligns to 2:459/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
39% identity, 83% coverage: 70:467/479 of query aligns to 23:443/450 of 4n0iA
- active site: K38 (= K82), S116 (= S157), S117 (= S158), T135 (≠ S176), T137 (= T178), G138 (= G179), G139 (= G180), S140 (= S181), L143 (≠ Q184)
- binding glutamine: G89 (= G133), T137 (= T178), G138 (= G179), S140 (= S181), Y168 (≠ F209), Y271 (= Y310), Y272 (= Y311), R320 (= R358), D404 (= D425)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
36% identity, 84% coverage: 72:474/479 of query aligns to 85:497/508 of 3a1iA
- active site: K95 (= K82), S170 (= S157), S171 (= S158), G189 (≠ S176), Q191 (≠ T178), G192 (= G179), G193 (= G180), A194 (≠ S181), I197 (≠ Q184)
- binding benzamide: F145 (≠ M132), S146 (≠ G133), G147 (≠ S134), Q191 (≠ T178), G192 (= G179), G193 (= G180), A194 (≠ S181), W327 (≠ Y310)
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, 92% coverage: 35:474/479 of query aligns to 158:588/607 of Q7XJJ7
- K205 (= K82) mutation to A: Loss of activity.
- SS 281:282 (= SS 157:158) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 178:181) binding
- S305 (= S181) mutation to A: Loss of activity.
- R307 (= R183) mutation to A: Loss of activity.
- S360 (≠ H236) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
29% identity, 92% coverage: 35:474/479 of query aligns to 158:588/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A131), T258 (≠ S134), S281 (= S157), G302 (≠ T178), G303 (= G179), S305 (= S181), S472 (≠ A349), I532 (≠ V415), M539 (≠ Y422)
Sites not aligning to the query:
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
35% identity, 97% coverage: 9:474/479 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)
33% identity, 96% coverage: 13:474/479 of query aligns to 10:476/487 of 1m21A
- active site: K81 (= K82), S160 (= S157), S161 (= S158), T179 (≠ S176), T181 (= T178), D182 (≠ G179), G183 (= G180), S184 (= S181), C187 (≠ Q184)
- binding : A129 (= A131), N130 (≠ M132), F131 (≠ G133), C158 (≠ G155), G159 (= G156), S160 (= S157), S184 (= S181), C187 (≠ Q184), I212 (≠ F209), R318 (≠ Y311), L321 (≠ A314), L365 (≠ M360), F426 (≠ V429)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
31% identity, 99% coverage: 4:475/479 of query aligns to 23:488/507 of Q84DC4
- T31 (≠ V12) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K82) mutation to A: Abolishes activity on mandelamide.
- S180 (= S157) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S158) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G179) 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 (= S181) mutation to A: Abolishes activity on mandelamide.
- Q207 (= Q184) 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 (≠ A306) 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 (vs. gap) 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 (≠ D425) 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.
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
34% identity, 96% coverage: 15:474/479 of query aligns to 11:468/482 of 3a2qA
- active site: K69 (= K82), S147 (= S157), S148 (= S158), N166 (≠ S176), A168 (≠ T178), A169 (≠ G179), G170 (= G180), A171 (≠ S181), I174 (≠ Q184)
- binding 6-aminohexanoic acid: G121 (≠ A131), G121 (≠ A131), N122 (≠ M132), S147 (= S157), A168 (≠ T178), A168 (≠ T178), A169 (≠ G179), A171 (≠ S181), C313 (≠ A314)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
31% identity, 96% coverage: 13:474/479 of query aligns to 6:407/412 of 1o9oA
- active site: K62 (= K82), A131 (≠ S157), S132 (= S158), T150 (≠ S176), T152 (= T178), G153 (= G179), G154 (= G180), S155 (= S181), R158 (≠ Q184)
- binding 3-amino-3-oxopropanoic acid: G130 (= G156), T152 (= T178), G153 (= G179), G154 (= G180), S155 (= S181), R158 (≠ Q184), P359 (≠ D425)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
31% identity, 96% coverage: 13:474/479 of query aligns to 6:407/412 of 1ocmA
- active site: K62 (= K82), S131 (= S157), S132 (= S158), T152 (= T178), G153 (= G179), G154 (= G180), S155 (= S181)
- binding pyrophosphate 2-: R113 (≠ G133), S131 (= S157), Q151 (≠ D177), T152 (= T178), G153 (= G179), G154 (= G180), S155 (= S181), R158 (≠ Q184), P359 (≠ D425)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
28% identity, 98% coverage: 9:479/479 of query aligns to 5:449/457 of 5h6sC
- active site: K77 (= K82), S152 (= S157), S153 (= S158), L173 (≠ T178), G174 (= G179), G175 (= G180), S176 (= S181)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A131), R128 (≠ G133), W129 (≠ S134), S152 (= S157), L173 (≠ T178), G174 (= G179), S176 (= S181), W306 (≠ Y310), F338 (≠ L361)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
34% identity, 87% coverage: 58:476/479 of query aligns to 51:444/461 of 4gysB
- active site: K72 (= K82), S146 (= S157), S147 (= S158), T165 (≠ S176), T167 (= T178), A168 (≠ G179), G169 (= G180), S170 (= S181), V173 (≠ Q184)
- binding malonate ion: A120 (= A131), G122 (= G133), S146 (= S157), T167 (= T178), A168 (≠ G179), S170 (= S181), S193 (≠ Y204), G194 (= G205), V195 (≠ L206), R200 (≠ S211), Y297 (≠ F325), R305 (= R333)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
33% identity, 84% coverage: 73:473/479 of query aligns to 82:460/605 of Q936X2
- K91 (= K82) mutation to A: Loss of activity.
- S165 (= S157) mutation to A: Loss of activity.
- S189 (= S181) mutation to A: Loss of activity.
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)
29% identity, 84% coverage: 74:475/479 of query aligns to 28:423/425 of Q9FR37
- K36 (= K82) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S157) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S158) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D177) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S181) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C189) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (≠ A259) mutation to T: Slightly reduces catalytic activity.
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
28% identity, 97% coverage: 11:474/479 of query aligns to 8:473/490 of 4yjiA
- active site: K79 (= K82), S158 (= S157), S159 (= S158), G179 (≠ T178), G180 (= G179), G181 (= G180), A182 (≠ S181)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ N84), G132 (≠ A131), S158 (= S157), G179 (≠ T178), G180 (= G179), A182 (≠ S181)
Query Sequence
>WP_015798951.1 NCBI__GCF_000023265.1:WP_015798951.1
MNSEAILDLGAVDIARAVREGAVRAEEVLEAYEAQVAVEEPEVHAFLHLDFDAARRRAAA
VDAAVRAGHDPGPLAGVPIAIKDNIVQEGVPTTAGSRILEGWVSPYSATVVDRVLAAGGV
IVGKTNLDEFAMGSSTENSAFGPTRNPHDLDRVPGGSSGGSAAAVAARFSALALGSDTGG
SIRQPASLCGVVGVKPTYGAISRYGLIAFASSLDQIGPFAATVDDAAALLAVLSGHDPRD
ATSAPRGPIVSDPSDRDVAGWTVGVVTELAETADPAVAAALEAAARHLERLGASVVSVSI
PEVAAALAAYYVVAPAEASSNLARFDGVRYGLRVEALTTDEMMVATRSAGFGDEVKRRIM
LGTYALSAGYRDALYVQAQRVRTWLAAGLARAFADVDVLITPTSPTTAFRLGERVADPVA
MYRSDVCTVPSNLVGGPAVSVPFGYDADRLPIGIQVMAPAWEDARMLVAARALEAGAER
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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