SitesBLAST
Comparing WP_011372405.1 NCBI__GCF_000012965.1:WP_011372405.1 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)
53% identity, 90% coverage: 44:445/447 of query aligns to 66:471/478 of 3h0mA
- active site: K72 (= K50), S147 (= S125), S148 (= S126), S166 (= S144), T168 (= T146), G169 (= G147), G170 (= G148), S171 (= S149), Q174 (= Q152)
- binding glutamine: M122 (= M100), G123 (= G101), D167 (= D145), T168 (= T146), G169 (= G147), G170 (= G148), S171 (= S149), F199 (≠ Y177), Y302 (= Y277), R351 (= R325), D418 (= D391)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
53% identity, 90% coverage: 44:445/447 of query aligns to 66:471/478 of 3h0lA
- active site: K72 (= K50), S147 (= S125), S148 (= S126), S166 (= S144), T168 (= T146), G169 (= G147), G170 (= G148), S171 (= S149), Q174 (= Q152)
- binding asparagine: G123 (= G101), S147 (= S125), G169 (= G147), G170 (= G148), S171 (= S149), Y302 (= Y277), R351 (= R325), D418 (= D391)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
52% identity, 90% coverage: 44:444/447 of query aligns to 73:477/485 of 2f2aA
- active site: K79 (= K50), S154 (= S125), S155 (= S126), S173 (= S144), T175 (= T146), G176 (= G147), G177 (= G148), S178 (= S149), Q181 (= Q152)
- binding glutamine: G130 (= G101), S154 (= S125), D174 (= D145), T175 (= T146), G176 (= G147), S178 (= S149), F206 (≠ Y177), Y309 (= Y277), Y310 (= Y278), R358 (= R325), D425 (= D391)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
52% identity, 90% coverage: 44:444/447 of query aligns to 73:477/485 of 2dqnA
- active site: K79 (= K50), S154 (= S125), S155 (= S126), S173 (= S144), T175 (= T146), G176 (= G147), G177 (= G148), S178 (= S149), Q181 (= Q152)
- binding asparagine: M129 (= M100), G130 (= G101), T175 (= T146), G176 (= G147), S178 (= S149), Y309 (= Y277), Y310 (= Y278), R358 (= R325), D425 (= D391)
3kfuE Crystal structure of the transamidosome (see paper)
45% identity, 95% coverage: 15:440/447 of query aligns to 17:454/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
34% identity, 96% coverage: 7:434/447 of query aligns to 1:444/450 of 4n0iA
- active site: K38 (= K50), S116 (= S125), S117 (= S126), T135 (≠ S144), T137 (= T146), G138 (= G147), G139 (= G148), S140 (= S149), L143 (≠ Q152)
- binding glutamine: G89 (= G101), T137 (= T146), G138 (= G147), S140 (= S149), Y168 (= Y177), Y271 (= Y277), Y272 (= Y278), R320 (= R325), D404 (= D391)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
30% identity, 89% coverage: 43:440/447 of query aligns to 198:588/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A99), T258 (≠ S102), S281 (= S125), G302 (≠ T146), G303 (= G147), S305 (= S149), S472 (≠ N330), I532 (≠ T383), M539 (≠ S390)
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)
30% identity, 89% coverage: 43:440/447 of query aligns to 198:588/607 of Q7XJJ7
- K205 (= K50) mutation to A: Loss of activity.
- SS 281:282 (= SS 125:126) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 146:149) binding substrate
- S305 (= S149) mutation to A: Loss of activity.
- R307 (= R151) mutation to A: Loss of activity.
- S360 (≠ H204) mutation to A: No effect.
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
30% identity, 89% coverage: 43:440/447 of query aligns to 198:588/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A99), G302 (≠ T146), G303 (= G147), G304 (= G148), A305 (≠ S149), V442 (≠ Y278), I475 (≠ L333), M539 (≠ S390)
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
30% identity, 89% coverage: 43:440/447 of query aligns to 198:588/605 of 8ey1D
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
33% identity, 86% coverage: 44:429/447 of query aligns to 68:437/457 of 6c6gA
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
31% identity, 85% coverage: 44:422/447 of query aligns to 94:469/507 of Q84DC4
- K100 (= K50) mutation to A: Abolishes activity on mandelamide.
- S180 (= S125) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S126) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G147) 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 (= S149) mutation to A: Abolishes activity on mandelamide.
- Q207 (= Q152) 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 (= S275) 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 (≠ E339) 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 (≠ L392) 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.
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
31% identity, 89% coverage: 44:442/447 of query aligns to 75:478/487 of 1m21A
- active site: K81 (= K50), S160 (= S125), S161 (= S126), T179 (≠ S144), T181 (= T146), D182 (≠ G147), G183 (= G148), S184 (= S149), C187 (≠ Q152)
- binding : A129 (= A99), N130 (vs. gap), F131 (vs. gap), C158 (≠ G123), G159 (= G124), S160 (= S125), S184 (= S149), C187 (≠ Q152), I212 (≠ Y177), R318 (≠ T287), L321 (≠ A290), L365 (= L327), F426 (≠ Y388)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
27% identity, 88% coverage: 47:441/447 of query aligns to 92:498/508 of 3a1iA
- active site: K95 (= K50), S170 (= S125), S171 (= S126), G189 (≠ S144), Q191 (≠ T146), G192 (= G147), G193 (= G148), A194 (≠ S149), I197 (≠ Q152)
- binding benzamide: F145 (≠ M100), S146 (≠ G101), G147 (≠ S102), Q191 (≠ T146), G192 (= G147), G193 (= G148), A194 (≠ S149), W327 (vs. gap)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
29% identity, 88% coverage: 44:438/447 of query aligns to 85:454/605 of Q936X2
- K91 (= K50) mutation to A: Loss of activity.
- S165 (= S125) mutation to A: Loss of activity.
- S189 (= S149) mutation to A: Loss of activity.
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
30% identity, 95% coverage: 24:447/447 of query aligns to 30:475/482 of 3a2qA
- active site: K69 (= K50), S147 (= S125), S148 (= S126), N166 (≠ S144), A168 (≠ T146), A169 (≠ G147), G170 (= G148), A171 (≠ S149), I174 (≠ Q152)
- binding 6-aminohexanoic acid: G121 (≠ A99), G121 (≠ A99), N122 (≠ M100), S147 (= S125), A168 (≠ T146), A168 (≠ T146), A169 (≠ G147), A171 (≠ S149), C313 (≠ Y278)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
29% identity, 90% coverage: 44:444/447 of query aligns to 66:442/461 of 4gysB
- active site: K72 (= K50), S146 (= S125), S147 (= S126), T165 (≠ S144), T167 (= T146), A168 (≠ G147), G169 (= G148), S170 (= S149), V173 (≠ Q152)
- binding malonate ion: A120 (= A99), G122 (= G101), S146 (= S125), T167 (= T146), A168 (≠ G147), S170 (= S149), S193 (≠ Y172), G194 (= G173), V195 (≠ L174), R200 (≠ S179), Y297 (= Y292), R305 (= R300)
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)
42% identity, 32% coverage: 44:185/447 of query aligns to 30:173/425 of Q9FR37
- K36 (= K50) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S125) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S126) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D145) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S149) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C157) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 214 S→T: Slightly reduces catalytic activity.
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
27% identity, 97% coverage: 7:440/447 of query aligns to 28:407/412 of 1o9oA
- active site: K62 (= K50), A131 (≠ S125), S132 (= S126), T150 (≠ S144), T152 (= T146), G153 (= G147), G154 (= G148), S155 (= S149), R158 (≠ Q152)
- binding 3-amino-3-oxopropanoic acid: G130 (= G124), T152 (= T146), G153 (= G147), G154 (= G148), S155 (= S149), R158 (≠ Q152), P359 (≠ E386)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
27% identity, 97% coverage: 7:440/447 of query aligns to 28:407/412 of 1ocmA
- active site: K62 (= K50), S131 (= S125), S132 (= S126), T152 (= T146), G153 (= G147), G154 (= G148), S155 (= S149)
- binding pyrophosphate 2-: R113 (≠ G101), S131 (= S125), Q151 (≠ D145), T152 (= T146), G153 (= G147), G154 (= G148), S155 (= S149), R158 (≠ Q152), P359 (≠ E386)
Query Sequence
>WP_011372405.1 NCBI__GCF_000012965.1:WP_011372405.1
MITLKEALKLSKDELENFKNDLKAKIEANPELNAYIDIYNIGDGVPIAIKDNIQVKDWSV
TSGSNILQGYIAPYNATVIEKMLSAGLSPFGRTNMDEFAMGSTTESSFYGKTLNPHNKDC
VPGGSSGGSAAAVGAGLAIAALGSDTGGSIRQPASFCGIVGMKPTYGRVSRYGLGAYASS
LDQIGPMTQNVEDAAILYDIISGHDEKDSTSAHKNDKVSDKLNPNRKIRIAVLPKHIQNA
SEDVKKAYELAINALKKVGHEIVEAELMDAKFDISAYYITATAEATTNLARYDGIRYGNR
VVGKDLNDTFVQTRSQGFGDEVKRRILLGNFVLSSGYYEAYYVKAQKTRHLIKDQYSKIF
ENVDLILSPVAPTTANKFGELSTPMEMYLSDLYTISVNLAGLPAISVPISKSSEGMPIGL
QLIANAYDEQTLFDGALSLEREINYNA
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