SitesBLAST
Comparing WP_013721506.1 NCBI__GCF_000204645.1:WP_013721506.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
29% identity, 95% coverage: 8:452/468 of query aligns to 7:473/485 of 2f2aA
- active site: K79 (= K80), S154 (= S155), S155 (= S156), S173 (≠ T174), T175 (≠ I176), G176 (= G177), G177 (= G178), S178 (= S179), Q181 (≠ L182)
- binding glutamine: G130 (≠ L131), S154 (= S155), D174 (= D175), T175 (≠ I176), G176 (= G177), S178 (= S179), F206 (≠ P203), Y309 (vs. gap), Y310 (vs. gap), R358 (≠ L333), D425 (≠ I403)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
29% identity, 95% coverage: 8:452/468 of query aligns to 7:473/485 of 2dqnA
- active site: K79 (= K80), S154 (= S155), S155 (= S156), S173 (≠ T174), T175 (≠ I176), G176 (= G177), G177 (= G178), S178 (= S179), Q181 (≠ L182)
- binding asparagine: M129 (= M130), G130 (≠ L131), T175 (≠ I176), G176 (= G177), S178 (= S179), Y309 (vs. gap), Y310 (vs. gap), R358 (≠ L333), D425 (≠ I403)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
32% identity, 99% coverage: 5:466/468 of query aligns to 4:483/490 of 4yjiA
- active site: K79 (= K80), S158 (= S155), S159 (= S156), G179 (≠ I176), G180 (= G177), G181 (= G178), A182 (≠ S179)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ N82), G132 (= G129), S158 (= S155), G179 (≠ I176), G180 (= G177), A182 (≠ S179)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
30% identity, 95% coverage: 8:453/468 of query aligns to 6:467/478 of 3h0mA
- active site: K72 (= K80), S147 (= S155), S148 (= S156), S166 (≠ T174), T168 (≠ I176), G169 (= G177), G170 (= G178), S171 (= S179), Q174 (≠ L182)
- binding glutamine: M122 (= M130), G123 (≠ L131), D167 (= D175), T168 (≠ I176), G169 (= G177), G170 (= G178), S171 (= S179), F199 (≠ P203), Y302 (≠ F300), R351 (≠ L333), D418 (≠ I403)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
30% identity, 95% coverage: 8:453/468 of query aligns to 6:467/478 of 3h0lA
- active site: K72 (= K80), S147 (= S155), S148 (= S156), S166 (≠ T174), T168 (≠ I176), G169 (= G177), G170 (= G178), S171 (= S179), Q174 (≠ L182)
- binding asparagine: G123 (≠ L131), S147 (= S155), G169 (= G177), G170 (= G178), S171 (= S179), Y302 (≠ F300), R351 (≠ L333), D418 (≠ I403)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
28% identity, 98% coverage: 7:464/468 of query aligns to 5:455/457 of 5h6sC
- active site: K77 (= K80), S152 (= S155), S153 (= S156), L173 (≠ I176), G174 (= G177), G175 (= G178), S176 (= S179)
- binding 4-oxidanylbenzohydrazide: C126 (≠ G129), R128 (≠ L131), W129 (≠ S132), S152 (= S155), L173 (≠ I176), G174 (= G177), S176 (= S179), W306 (vs. gap), F338 (≠ W339)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
31% identity, 83% coverage: 70:456/468 of query aligns to 85:501/508 of 3a1iA
- active site: K95 (= K80), S170 (= S155), S171 (= S156), G189 (≠ T174), Q191 (≠ I176), G192 (= G177), G193 (= G178), A194 (≠ S179), I197 (≠ L182)
- binding benzamide: F145 (≠ M130), S146 (≠ L131), G147 (≠ S132), Q191 (≠ I176), G192 (= G177), G193 (= G178), A194 (≠ S179), W327 (= W313)
3kfuE Crystal structure of the transamidosome (see paper)
32% identity, 93% coverage: 20:453/468 of query aligns to 13:455/468 of 3kfuE
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, 94% coverage: 15:454/468 of query aligns to 137:590/607 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 (≠ IGGS 176:179) binding
- S305 (= S179) mutation to A: Loss of activity.
- R307 (= R181) mutation to A: Loss of activity.
- S360 (≠ P230) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
29% identity, 94% coverage: 15:454/468 of query aligns to 137:590/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (= G129), T258 (≠ S132), S281 (= S155), G302 (≠ I176), G303 (= G177), S305 (= S179), S472 (= S342), I532 (vs. gap), M539 (≠ I403)
Sites not aligning to the query:
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
29% identity, 97% coverage: 6:460/468 of query aligns to 5:484/487 of 1m21A
- active site: K81 (= K80), S160 (= S155), S161 (= S156), T179 (= T174), T181 (≠ I176), D182 (≠ G177), G183 (= G178), S184 (= S179), C187 (≠ L182)
- binding : A129 (≠ G129), N130 (≠ M130), F131 (≠ L131), C158 (≠ G153), G159 (= G154), S160 (= S155), S184 (= S179), C187 (≠ L182), I212 (≠ P203), R318 (vs. gap), L321 (= L301), L365 (≠ A340), F426 (≠ R398)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
34% identity, 55% coverage: 7:263/468 of query aligns to 1:260/457 of 6c6gA
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)
32% identity, 64% coverage: 11:309/468 of query aligns to 81:375/579 of Q9TUI8
- S217 (= S155) mutation to A: Loss of activity.
- S218 (= S156) mutation to A: Lowers activity by at least 98%.
- D237 (= D175) mutation D->E,N: Loss of activity.
- S241 (= S179) mutation to A: Loss of activity.
- C249 (= C187) mutation to A: Loss of activity.
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
26% identity, 87% coverage: 46:453/468 of query aligns to 58:462/605 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.
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
31% identity, 62% coverage: 6:294/468 of query aligns to 27:304/507 of Q84DC4
- T31 (≠ S10) 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 (≠ L182) 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.
Sites not aligning to the query:
- 316 S→N: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with H-207 and N-437.
- 382 Q→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.
- 437 I→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)
32% identity, 55% coverage: 17:275/468 of query aligns to 15:273/482 of 3a2qA
- active site: K69 (= K80), S147 (= S155), S148 (= S156), N166 (≠ T174), A168 (≠ I176), A169 (≠ G177), G170 (= G178), A171 (≠ S179), I174 (≠ L182)
- binding 6-aminohexanoic acid: G121 (= G129), G121 (= G129), N122 (≠ M130), S147 (= S155), A168 (≠ I176), A168 (≠ I176), A169 (≠ G177), A171 (≠ S179)
Sites not aligning to the query:
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
32% identity, 48% coverage: 6:231/468 of query aligns to 4:240/564 of 6te4A
Sites not aligning to the query:
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
27% identity, 92% coverage: 11:441/468 of query aligns to 6:427/461 of 4gysB
- active site: K72 (= K80), S146 (= S155), S147 (= S156), T165 (= T174), T167 (≠ I176), A168 (≠ G177), G169 (= G178), S170 (= S179), V173 (≠ L182)
- binding malonate ion: A120 (≠ G129), G122 (≠ L131), S146 (= S155), T167 (≠ I176), A168 (≠ G177), S170 (= S179), S193 (≠ D202), G194 (≠ P203), V195 (≠ P204), R200 (= R208), Y297 (≠ P296), R305 (≠ H304)
4hbpA Crystal structure of faah in complex with inhibitor (see paper)
33% identity, 55% coverage: 44:299/468 of query aligns to 63:323/531 of 4hbpA
- active site: K100 (= K80), S175 (= S155), S176 (= S156), T194 (= T174), I196 (= I176), G197 (= G177), G198 (= G178), S199 (= S179), F202 (≠ L182)
- binding 4-(3-phenyl-1,2,4-thiadiazol-5-yl)-N-(pyridin-3-yl)piperazine-1-carboxamide: S151 (= S132), F152 (≠ S133), I196 (= I176), G197 (= G177), S199 (= S179)
Sites not aligning to the query:
4do3A Structure of faah with a non-steroidal anti-inflammatory drug (see paper)
34% identity, 49% coverage: 70:299/468 of query aligns to 100:333/543 of 4do3A
- active site: K110 (= K80), S185 (= S155), S186 (= S156), T204 (= T174), I206 (= I176), G207 (= G177), G208 (= G178), S209 (= S179), F212 (≠ L182)
- binding (2S)-2-(6-chloro-9H-carbazol-2-yl)propanoic acid: L160 (= L131)
- binding cyclohexane aminocarboxylic acid: L160 (= L131), I206 (= I176), G207 (= G177), S209 (= S179)
Sites not aligning to the query:
Query Sequence
>WP_013721506.1 NCBI__GCF_000204645.1:WP_013721506.1
MSAPHDLSASELLAAYRARSLSPVEATQSVLDHIARWEPHLHATYLLRPEEALAQARASE
ARWLRGAPCGPLDGVPATVKDNIATRGDPTPLGTAATPLMPAPADAPPAARLREAGAVIV
CKTTMPDYGMLSSGLSSFHALARNPWDLSRGPGGSSAGAGAAAAAGYGPLHVGTDIGGSI
RLPAGWCGVFGLKPSLGRIPIDPPYTGRAAGPMTRTVQDAALMMQVLSAPDARDSMSLPA
QPIAWDDFGQGPGRLRGLRIGLLLDAGCGLPVDPQVRAAVEAAARLFEQAGAAIEPMPPF
LTRHMLDGMDHFWRMRSFMDLRTLTPGQQGKVLPFIRDWAMSAAGLDGPQVFEASQQFHA
TRVATVHACAPFDYVLSPVAPMPAFAAELPAPTDDPLRPLEHIAFTVPFNMSEQPAASVN
CGYTGGGLPIGLQIAGRRFDDLGVLQMAHAFEQLRGPQRPWPEPPDRH
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