SitesBLAST
Comparing WP_152617830.1 NCBI__GCF_000744815.1:WP_152617830.1 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)
31% identity, 95% coverage: 12:464/476 of query aligns to 14:476/478 of 3h0mA
- active site: K72 (= K76), S147 (= S153), S148 (= S154), S166 (≠ T172), T168 (= T174), G169 (≠ A175), G170 (= G176), S171 (= S177), Q174 (≠ I180)
- binding glutamine: M122 (≠ I128), G123 (= G129), D167 (= D173), T168 (= T174), G169 (≠ A175), G170 (= G176), S171 (= S177), F199 (≠ L205), Y302 (≠ D313), R351 (= R341), D418 (≠ G404)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
31% identity, 95% coverage: 12:464/476 of query aligns to 14:476/478 of 3h0lA
- active site: K72 (= K76), S147 (= S153), S148 (= S154), S166 (≠ T172), T168 (= T174), G169 (≠ A175), G170 (= G176), S171 (= S177), Q174 (≠ I180)
- binding asparagine: G123 (= G129), S147 (= S153), G169 (≠ A175), G170 (= G176), S171 (= S177), Y302 (≠ D313), R351 (= R341), D418 (≠ G404)
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
33% identity, 86% coverage: 40:447/476 of query aligns to 168:581/607 of Q7XJJ7
- K205 (= K76) mutation to A: Loss of activity.
- SS 281:282 (= SS 153:154) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TAGS 174:177) binding substrate
- S305 (= S177) mutation to A: Loss of activity.
- R307 (= R179) mutation to A: Loss of activity.
- S360 (≠ P232) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
33% identity, 86% coverage: 40:447/476 of query aligns to 168:581/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A127), T258 (≠ S130), S281 (= S153), G302 (≠ T174), G303 (≠ A175), S305 (= S177), S472 (≠ T343), I532 (≠ V398), M539 (≠ G405)
Sites not aligning to the query:
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
32% identity, 86% coverage: 40:447/476 of query aligns to 168:581/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A127), G302 (≠ T174), G303 (≠ A175), G304 (= G176), A305 (≠ S177), V442 (≠ M314), I475 (≠ S346), M539 (≠ G405)
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
32% identity, 86% coverage: 40:447/476 of query aligns to 168:581/605 of 8ey1D
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
29% identity, 96% coverage: 3:461/476 of query aligns to 6:478/485 of 2f2aA
- active site: K79 (= K76), S154 (= S153), S155 (= S154), S173 (≠ T172), T175 (= T174), G176 (≠ A175), G177 (= G176), S178 (= S177), Q181 (≠ I180)
- binding glutamine: G130 (= G129), S154 (= S153), D174 (= D173), T175 (= T174), G176 (≠ A175), S178 (= S177), F206 (≠ L205), Y309 (= Y306), Y310 (≠ A307), R358 (vs. gap), D425 (≠ G404)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
29% identity, 96% coverage: 3:461/476 of query aligns to 6:478/485 of 2dqnA
- active site: K79 (= K76), S154 (= S153), S155 (= S154), S173 (≠ T172), T175 (= T174), G176 (≠ A175), G177 (= G176), S178 (= S177), Q181 (≠ I180)
- binding asparagine: M129 (≠ I128), G130 (= G129), T175 (= T174), G176 (≠ A175), S178 (= S177), Y309 (= Y306), Y310 (≠ A307), R358 (vs. gap), D425 (≠ G404)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
33% identity, 93% coverage: 14:454/476 of query aligns to 12:448/457 of 6c6gA
3kfuE Crystal structure of the transamidosome (see paper)
33% identity, 95% coverage: 15:464/476 of query aligns to 12:465/468 of 3kfuE
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
31% identity, 94% coverage: 10:457/476 of query aligns to 13:479/487 of 1m21A
- active site: K81 (= K76), S160 (= S153), S161 (= S154), T179 (= T172), T181 (= T174), D182 (≠ A175), G183 (= G176), S184 (= S177), C187 (≠ I180)
- binding : A129 (= A127), N130 (vs. gap), F131 (≠ I128), C158 (≠ G151), G159 (= G152), S160 (= S153), S184 (= S177), C187 (≠ I180), I212 (≠ L205), R318 (≠ M314), L321 (≠ M317), L365 (≠ T340), F426 (= F403)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
34% identity, 74% coverage: 103:455/476 of query aligns to 120:498/508 of 3a1iA
- active site: S170 (= S153), S171 (= S154), G189 (≠ T172), Q191 (≠ T174), G192 (≠ A175), G193 (= G176), A194 (≠ S177), I197 (= I180)
- binding benzamide: F145 (≠ I128), S146 (vs. gap), G147 (= G129), Q191 (≠ T174), G192 (≠ A175), G193 (= G176), A194 (≠ S177), W327 (vs. gap)
Sites not aligning to the query:
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
29% identity, 95% coverage: 4:456/476 of query aligns to 6:446/457 of 5h6sC
- active site: K77 (= K76), S152 (= S153), S153 (= S154), L173 (≠ T174), G174 (≠ A175), G175 (= G176), S176 (= S177)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A127), R128 (≠ G129), W129 (≠ S130), S152 (= S153), L173 (≠ T174), G174 (≠ A175), S176 (= S177), W306 (≠ Y306), F338 (= F348)
Q9AHE8 Urethanase; Enantioselective amidase; Ethyl carbamate-degrading amidase; EC 3.5.1.75 from Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium radiobacter) (see 3 papers)
29% identity, 80% coverage: 62:444/476 of query aligns to 84:499/517 of Q9AHE8
- R94 (≠ P72) mutation to P: No change in activity.
- I97 (≠ V75) mutation to L: 1.12-fold increase in specific activity toward ethyl carbamate, shows higher ethanol tolerance. 3.1-fold increase in specific activity toward ethyl carbamate and 1.5-fold increase in ethanol tolerance, shows lower pH tolerance; when associated with A-195.
- K98 (= K76) mutation to A: Almost loss of activity.
- P163 (= P143) mutation to A: Decrease in activity.
- A172 (≠ G152) mutation to G: Changes substrate specificity. Decrease in activity.
- S173 (= S153) mutation to A: Almost loss of activity.
- N175 (≠ S155) mutation to G: Decrease in activity.; mutation to S: Changes substrate specificity.
- G195 (≠ A175) mutation to A: 1.86-fold increase in specific activity toward ethyl carbamate, shows lower pH tolerance, causes a decrease in the thermostability. 3.1-fold increase in specific activity toward ethyl carbamate and 1.5-fold increase in ethanol tolerance, shows lower pH tolerance; when associated with L-97.
- S197 (= S177) mutation to A: Almost loss of activity.
- L200 (≠ I180) mutation to C: Decrease in activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
32% identity, 87% coverage: 43:456/476 of query aligns to 42:440/461 of 4gysB
- active site: K72 (= K76), S146 (= S153), S147 (= S154), T165 (= T172), T167 (= T174), A168 (= A175), G169 (= G176), S170 (= S177), V173 (≠ I180)
- binding malonate ion: A120 (= A127), G122 (= G129), S146 (= S153), T167 (= T174), A168 (= A175), S170 (= S177), S193 (= S200), G194 (= G201), V195 (≠ C202), R200 (≠ Y207), Y297 (≠ T310), R305 (≠ L318)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
27% identity, 93% coverage: 6:449/476 of query aligns to 8:463/482 of 3a2qA
- active site: K69 (= K76), S147 (= S153), S148 (= S154), N166 (≠ T172), A168 (≠ T174), A169 (= A175), G170 (= G176), A171 (≠ S177), I174 (= I180)
- binding 6-aminohexanoic acid: G121 (≠ A127), G121 (≠ A127), N122 (≠ I128), S147 (= S153), A168 (≠ T174), A168 (≠ T174), A169 (= A175), A171 (≠ S177), C313 (≠ A307)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
35% identity, 68% coverage: 4:326/476 of query aligns to 29:327/507 of Q84DC4
- T31 (= T6) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K76) mutation to A: Abolishes activity on mandelamide.
- S180 (= S153) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S154) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ A175) 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 (= S177) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ I180) 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 (≠ T310) 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.
Sites not aligning to the query:
- 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.
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
32% identity, 85% coverage: 45:447/476 of query aligns to 32:400/412 of 1ocmA
- active site: K62 (= K76), S131 (= S153), S132 (= S154), T152 (= T174), G153 (≠ A175), G154 (= G176), S155 (= S177)
- binding pyrophosphate 2-: R113 (≠ P131), S131 (= S153), Q151 (≠ D173), T152 (= T174), G153 (≠ A175), G154 (= G176), S155 (= S177), R158 (≠ I180), P359 (≠ G405)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
31% identity, 85% coverage: 45:447/476 of query aligns to 32:400/412 of 1o9oA
- active site: K62 (= K76), A131 (≠ S153), S132 (= S154), T150 (= T172), T152 (= T174), G153 (≠ A175), G154 (= G176), S155 (= S177), R158 (≠ I180)
- binding 3-amino-3-oxopropanoic acid: G130 (= G152), T152 (= T174), G153 (≠ A175), G154 (= G176), S155 (= S177), R158 (≠ I180), P359 (≠ G405)
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)
37% identity, 33% coverage: 68:225/476 of query aligns to 28:190/425 of Q9FR37
- K36 (= K76) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S153) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S154) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D173) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S177) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C185) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 214 S→T: Slightly reduces catalytic activity.
Query Sequence
>WP_152617830.1 NCBI__GCF_000744815.1:WP_152617830.1
MPSTVTAAAAALRAGTVTSTALVEHAVRTADRLDPRVGSFISRYREESLAAAARADADFA
AGTDRGPLQGIPFGVKDIIASTDGPTTAQSLVLDPAWGEETGDAVVVSRLRAAGAIVVGK
ASTMEFAIGSPDPEKPFPIPANPWDLERWAGGSSSGTGSGVAAGMFLAGLGTDTAGSIRI
PSAYCGITGLKPTFGRVPKSGCVPLGYTLDNIGPMARSAADCALLLGLIAGPDASDHYSA
DVQVDDYSGALADGAGDLSGLTIGVDDLVAASDGHVDPAFRARFDAALGELAAAGARIVP
LSLPLYAELTAADMVVMLSEALAYHQGDLSRRWADYGAGTRMTVGSGFAFTGADYVQAQR
VRRVGQRMVAGLLEGVDAIVTPTSTLPAPRLDEFADRVPLLSFGGLHTPYWNSVGNPTLA
VPIGPAADGLPLSMQISTRPFAEALALRVGDAYQRRTAHHLSVPPLALAEPVAAVN
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