SitesBLAST
Comparing WP_012049314.1 NCBI__GCF_000016765.1:WP_012049314.1 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)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
30% identity, 91% coverage: 47:519/521 of query aligns to 1:457/457 of 5h6sC
- active site: K77 (= K125), S152 (= S200), S153 (= S201), L173 (≠ F221), G174 (≠ A222), G175 (= G223), S176 (= S224)
- binding 4-oxidanylbenzohydrazide: C126 (≠ G174), R128 (≠ G176), W129 (≠ S177), S152 (= S200), L173 (≠ F221), G174 (≠ A222), S176 (= S224), W306 (= W354), F338 (≠ E385)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
31% identity, 88% coverage: 49:509/521 of query aligns to 3:476/490 of 4yjiA
- active site: K79 (= K125), S158 (= S200), S159 (= S201), G179 (≠ F221), G180 (≠ A222), G181 (= G223), A182 (≠ S224)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L127), G132 (= G174), S158 (= S200), G179 (≠ F221), G180 (≠ A222), A182 (≠ S224)
3kfuE Crystal structure of the transamidosome (see paper)
35% identity, 87% coverage: 53:507/521 of query aligns to 2:455/468 of 3kfuE
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 87% coverage: 54:507/521 of query aligns to 8:467/478 of 3h0mA
- active site: K72 (= K125), S147 (= S200), S148 (= S201), S166 (= S219), T168 (≠ F221), G169 (≠ A222), G170 (= G223), S171 (= S224), Q174 (≠ N227)
- binding glutamine: M122 (≠ L175), G123 (= G176), D167 (= D220), T168 (≠ F221), G169 (≠ A222), G170 (= G223), S171 (= S224), F199 (= F253), Y302 (≠ A356), R351 (≠ E389), D418 (= D451)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 87% coverage: 54:507/521 of query aligns to 8:467/478 of 3h0lA
- active site: K72 (= K125), S147 (= S200), S148 (= S201), S166 (= S219), T168 (≠ F221), G169 (≠ A222), G170 (= G223), S171 (= S224), Q174 (≠ N227)
- binding asparagine: G123 (= G176), S147 (= S200), G169 (≠ A222), G170 (= G223), S171 (= S224), Y302 (≠ A356), R351 (≠ E389), D418 (= D451)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
28% identity, 92% coverage: 38:517/521 of query aligns to 15:494/507 of Q84DC4
- T31 (≠ A54) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K125) mutation to A: Abolishes activity on mandelamide.
- S180 (= S200) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S201) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ A222) 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 (= S224) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ N227) 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 (≠ D349) 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 (≠ N403) 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 (≠ M457) 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.
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
27% identity, 87% coverage: 52:506/521 of query aligns to 7:473/485 of 2f2aA
- active site: K79 (= K125), S154 (= S200), S155 (= S201), S173 (= S219), T175 (≠ F221), G176 (≠ A222), G177 (= G223), S178 (= S224), Q181 (≠ N227)
- binding glutamine: G130 (= G176), S154 (= S200), D174 (= D220), T175 (≠ F221), G176 (≠ A222), S178 (= S224), F206 (= F253), Y309 (vs. gap), Y310 (vs. gap), R358 (≠ E389), D425 (= D451)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
27% identity, 87% coverage: 52:506/521 of query aligns to 7:473/485 of 2dqnA
- active site: K79 (= K125), S154 (= S200), S155 (= S201), S173 (= S219), T175 (≠ F221), G176 (≠ A222), G177 (= G223), S178 (= S224), Q181 (≠ N227)
- binding asparagine: M129 (≠ L175), G130 (= G176), T175 (≠ F221), G176 (≠ A222), S178 (= S224), Y309 (vs. gap), Y310 (vs. gap), R358 (≠ E389), D425 (= D451)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
27% identity, 92% coverage: 41:520/521 of query aligns to 119:600/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (= G174), T258 (≠ S177), S281 (= S200), G302 (≠ F221), G303 (≠ A222), S305 (= S224), S472 (≠ E389), I532 (= I445), M539 (= M457)
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, 92% coverage: 41:520/521 of query aligns to 119:600/607 of Q7XJJ7
- K205 (= K125) mutation to A: Loss of activity.
- SS 281:282 (= SS 200:201) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ FAGS 221:224) binding
- S305 (= S224) mutation to A: Loss of activity.
- R307 (= R226) mutation to A: Loss of activity.
- S360 (≠ Y280) mutation to A: No effect.
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
31% identity, 76% coverage: 115:510/521 of query aligns to 85:501/508 of 3a1iA
- active site: K95 (= K125), S170 (= S200), S171 (= S201), G189 (≠ S219), Q191 (≠ F221), G192 (≠ A222), G193 (= G223), A194 (≠ S224), I197 (≠ N227)
- binding benzamide: F145 (≠ L175), S146 (≠ G176), G147 (≠ S177), Q191 (≠ F221), G192 (≠ A222), G193 (= G223), A194 (≠ S224), W327 (= W354)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
32% identity, 86% coverage: 60:508/521 of query aligns to 10:450/457 of 6c6gA
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
31% identity, 87% coverage: 54:507/521 of query aligns to 9:477/487 of 1m21A
- active site: K81 (= K125), S160 (= S200), S161 (= S201), T179 (≠ S219), T181 (≠ F221), D182 (≠ A222), G183 (= G223), S184 (= S224), C187 (≠ N227)
- binding : A129 (≠ G174), N130 (vs. gap), F131 (vs. gap), C158 (≠ G198), G159 (= G199), S160 (= S200), S184 (= S224), C187 (≠ N227), I212 (≠ E251), R318 (≠ H350), L321 (= L353), L365 (vs. gap), F426 (≠ Y453)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
37% identity, 43% coverage: 57:280/521 of query aligns to 11:229/482 of 3a2qA
- active site: K69 (= K125), S147 (= S200), S148 (= S201), N166 (≠ S219), A168 (≠ F221), A169 (= A222), G170 (= G223), A171 (≠ S224), I174 (≠ N227)
- binding 6-aminohexanoic acid: G121 (= G174), G121 (= G174), N122 (≠ L175), S147 (= S200), A168 (≠ F221), A168 (≠ F221), A169 (= A222), A171 (≠ S224)
Sites not aligning to the query:
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
29% identity, 75% coverage: 117:507/521 of query aligns to 83:462/605 of Q936X2
- K91 (= K125) mutation to A: Loss of activity.
- S165 (= S200) mutation to A: Loss of activity.
- S189 (= S224) mutation to A: Loss of activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
28% identity, 83% coverage: 66:495/521 of query aligns to 17:427/461 of 4gysB
- active site: K72 (= K125), S146 (= S200), S147 (= S201), T165 (≠ S219), T167 (≠ F221), A168 (= A222), G169 (= G223), S170 (= S224), V173 (≠ N227)
- binding malonate ion: A120 (≠ G174), G122 (= G176), S146 (= S200), T167 (≠ F221), A168 (= A222), S170 (= S224), S193 (≠ G247), G194 (≠ P248), V195 (≠ T249), R200 (≠ Q255), Y297 (≠ A366), R305 (vs. gap)
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
33% identity, 46% coverage: 47:284/521 of query aligns to 1:243/564 of 6te4A
Sites not aligning to the query:
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
26% identity, 74% coverage: 117:501/521 of query aligns to 30:445/450 of 4n0iA
- active site: K38 (= K125), S116 (= S200), S117 (= S201), T135 (≠ S219), T137 (≠ F221), G138 (≠ A222), G139 (= G223), S140 (= S224), L143 (≠ N227)
- binding glutamine: G89 (= G176), T137 (≠ F221), G138 (≠ A222), S140 (= S224), Y168 (≠ F253), Y271 (vs. gap), Y272 (vs. gap), R320 (≠ G393), D404 (≠ E458)
Q9TUI8 Fatty-acid amide hydrolase 1; Anandamide amidase; Anandamide amidohydrolase 1; Fatty acid ester hydrolase; Oleamide hydrolase 1; EC 3.5.1.99; EC 3.1.1.- from Sus scrofa (Pig) (see paper)
26% identity, 55% coverage: 55:343/521 of query aligns to 81:362/579 of Q9TUI8
- S217 (= S200) mutation to A: Loss of activity.
- S218 (= S201) mutation to A: Lowers activity by at least 98%.
- D237 (= D220) mutation D->E,N: Loss of activity.
- S241 (= S224) mutation to A: Loss of activity.
- C249 (≠ N232) mutation to A: Loss of activity.
4do3A Structure of faah with a non-steroidal anti-inflammatory drug (see paper)
26% identity, 55% coverage: 59:343/521 of query aligns to 53:330/543 of 4do3A
- active site: K110 (= K125), S185 (= S200), S186 (= S201), T204 (≠ S219), I206 (≠ F221), G207 (≠ A222), G208 (= G223), S209 (= S224), F212 (≠ N227)
- binding (2S)-2-(6-chloro-9H-carbazol-2-yl)propanoic acid: L160 (= L175)
- binding cyclohexane aminocarboxylic acid: L160 (= L175), I206 (≠ F221), G207 (≠ A222), S209 (= S224)
Sites not aligning to the query:
Query Sequence
>WP_012049314.1 NCBI__GCF_000016765.1:WP_012049314.1
MTRDSSATTDFSRRDALLAGVASATMLAGAGAAEARVAGRRAAPPPEIVTWTAADLAARI
RSRAVSCREVMTAHLDWIDRANPALNAIVSRVERPALLAAADEADREIAAGRHRGWMHGL
PHAVKDLAATRGIRTTMGSPIFADNVPKADEIFVERLRAAGAILIGKTNVPEFGLGSQSY
NPVFGVTRNAYDPSRTAGGSSGGAAAALAARMVPVADGSDFAGSLRNPAGWNNIFGFRPS
AGRVPHGPTNELFVQNIGYEGPMARTVGDLALLLSVMAGYDARTPLSLDGDPAVFAGPLD
RDMKGVRIGWLGDLGGVPMAPGMLDLCLSGLRRLEAAGCVIEPVSLDIDHDTLWKAFVQL
RQGFLAGGLGPLYADPARRKLLKPEAVWEIENGMKLSAVDLYNASVVRSRVYEAYRKAFE
RHDFLALPSAQLFPFDADLHWPKEIAGVAMDSYHRWMEIVAGPSLTGCPALCVPAGFGPE
GLPSGLQLVGPSRQDLAVLQLGRAYEQVAGDILGRKPALLG
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