SitesBLAST
Comparing WP_101444719.1 NCBI__GCF_002846395.1:WP_101444719.1 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)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
30% identity, 77% coverage: 115:544/555 of query aligns to 3:480/485 of 2f2aA
- active site: K79 (= K191), S154 (= S263), S155 (= S264), S173 (≠ T282), T175 (= T284), G176 (≠ L285), G177 (= G286), S178 (= S287), Q181 (≠ S290)
- binding glutamine: G130 (= G242), S154 (= S263), D174 (≠ E283), T175 (= T284), G176 (≠ L285), S178 (= S287), F206 (≠ L315), Y309 (≠ R409), Y310 (≠ D410), R358 (≠ N441), D425 (≠ N491)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
30% identity, 77% coverage: 115:544/555 of query aligns to 3:480/485 of 2dqnA
- active site: K79 (= K191), S154 (= S263), S155 (= S264), S173 (≠ T282), T175 (= T284), G176 (≠ L285), G177 (= G286), S178 (= S287), Q181 (≠ S290)
- binding asparagine: M129 (= M241), G130 (= G242), T175 (= T284), G176 (≠ L285), S178 (= S287), Y309 (≠ R409), Y310 (≠ D410), R358 (≠ N441), D425 (≠ N491)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
31% identity, 77% coverage: 119:548/555 of query aligns to 6:476/478 of 3h0mA
- active site: K72 (= K191), S147 (= S263), S148 (= S264), S166 (≠ T282), T168 (= T284), G169 (≠ L285), G170 (= G286), S171 (= S287), Q174 (≠ S290)
- binding glutamine: M122 (= M241), G123 (= G242), D167 (≠ E283), T168 (= T284), G169 (≠ L285), G170 (= G286), S171 (= S287), F199 (≠ L315), Y302 (≠ L413), R351 (vs. gap), D418 (vs. gap)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
31% identity, 77% coverage: 119:548/555 of query aligns to 6:476/478 of 3h0lA
- active site: K72 (= K191), S147 (= S263), S148 (= S264), S166 (≠ T282), T168 (= T284), G169 (≠ L285), G170 (= G286), S171 (= S287), Q174 (≠ S290)
- binding asparagine: G123 (= G242), S147 (= S263), G169 (≠ L285), G170 (= G286), S171 (= S287), Y302 (≠ L413), R351 (vs. gap), D418 (vs. gap)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
33% identity, 75% coverage: 131:549/555 of query aligns to 19:485/487 of 1m21A
- active site: K81 (= K191), S160 (= S263), S161 (= S264), T179 (= T282), T181 (= T284), D182 (≠ L285), G183 (= G286), S184 (= S287), C187 (≠ S290)
- binding : A129 (= A240), N130 (vs. gap), F131 (vs. gap), C158 (≠ S261), G159 (= G262), S160 (= S263), S184 (= S287), C187 (≠ S290), I212 (≠ L315), R318 (vs. gap), L321 (vs. gap), L365 (= L434), F426 (= F487)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
28% identity, 76% coverage: 117:540/555 of query aligns to 128:590/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A240), T258 (≠ D243), S281 (= S263), G302 (≠ T284), G303 (≠ L285), S305 (= S287), S472 (≠ A442), I532 (≠ L492), M539 (vs. gap)
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)
28% identity, 76% coverage: 117:540/555 of query aligns to 128:590/607 of Q7XJJ7
- K205 (= K191) mutation to A: Loss of activity.
- SS 281:282 (= SS 263:264) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TLGS 284:287) binding substrate
- S305 (= S287) mutation to A: Loss of activity.
- R307 (≠ V289) mutation to A: Loss of activity.
- S360 (≠ P342) mutation to A: No effect.
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
27% identity, 76% coverage: 117:540/555 of query aligns to 128:590/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A240), G302 (≠ T284), G303 (≠ L285), G304 (= G286), A305 (≠ S287), V442 (≠ T414), I475 (= I446), M539 (vs. gap)
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
27% identity, 76% coverage: 117:540/555 of query aligns to 128:590/605 of 8ey1D
3kfuE Crystal structure of the transamidosome (see paper)
28% identity, 77% coverage: 123:550/555 of query aligns to 1:466/468 of 3kfuE
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
27% identity, 75% coverage: 122:539/555 of query aligns to 5:449/457 of 6c6gA
Q9AHE8 Urethanase; Enantioselective amidase; Ethyl carbamate-degrading amidase; EC 3.5.1.75 from Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium radiobacter) (see 3 papers)
25% identity, 80% coverage: 87:531/555 of query aligns to 3:502/517 of Q9AHE8
- R94 (≠ P187) mutation to P: No change in activity.
- I97 (≠ V190) 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 (= K191) mutation to A: Almost loss of activity.
- P163 (= P253) mutation to A: Decrease in activity.
- A172 (≠ G262) mutation to G: Changes substrate specificity. Decrease in activity.
- S173 (= S263) mutation to A: Almost loss of activity.
- N175 (≠ A265) mutation to G: Decrease in activity.; mutation to S: Changes substrate specificity.
- G195 (≠ L285) 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 (= S287) mutation to A: Almost loss of activity.
- L200 (≠ S290) mutation to C: Decrease in activity.
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
28% identity, 67% coverage: 169:539/555 of query aligns to 41:408/412 of 1o9oA
- active site: K62 (= K191), A131 (≠ S263), S132 (= S264), T150 (= T282), T152 (= T284), G153 (≠ L285), G154 (= G286), S155 (= S287), R158 (≠ S290)
- binding 3-amino-3-oxopropanoic acid: G130 (= G262), T152 (= T284), G153 (≠ L285), G154 (= G286), S155 (= S287), R158 (≠ S290), P359 (vs. gap)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
28% identity, 67% coverage: 169:539/555 of query aligns to 41:408/412 of 1ocmA
- active site: K62 (= K191), S131 (= S263), S132 (= S264), T152 (= T284), G153 (≠ L285), G154 (= G286), S155 (= S287)
- binding pyrophosphate 2-: R113 (≠ G242), S131 (= S263), Q151 (≠ E283), T152 (= T284), G153 (≠ L285), G154 (= G286), S155 (= S287), R158 (≠ S290), P359 (vs. gap)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
25% identity, 77% coverage: 113:540/555 of query aligns to 23:489/507 of Q84DC4
- T31 (≠ P121) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K191) mutation to A: Abolishes activity on mandelamide.
- S180 (= S263) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S264) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ L285) 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 (= S287) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ S290) 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 (≠ D410) 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 (vs. gap) 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.
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
26% identity, 65% coverage: 181:540/555 of query aligns to 85:499/508 of 3a1iA
- active site: K95 (= K191), S170 (= S263), S171 (= S264), G189 (≠ T282), Q191 (≠ T284), G192 (≠ L285), G193 (= G286), A194 (≠ S287), I197 (≠ S290)
- binding benzamide: F145 (≠ M241), S146 (≠ G242), G147 (≠ D243), Q191 (≠ T284), G192 (≠ L285), G193 (= G286), A194 (≠ S287), W327 (≠ T412)
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)
29% identity, 54% coverage: 111:407/555 of query aligns to 70:369/579 of Q9TUI8
- S217 (= S263) mutation to A: Loss of activity.
- S218 (= S264) mutation to A: Lowers activity by at least 98%.
- D237 (≠ E283) mutation D->E,N: Loss of activity.
- S241 (= S287) mutation to A: Loss of activity.
- C249 (= C295) mutation to A: Loss of activity.
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
31% identity, 44% coverage: 183:428/555 of query aligns to 30:285/450 of 4n0iA
- active site: K38 (= K191), S116 (= S263), S117 (= S264), T135 (= T282), T137 (= T284), G138 (≠ L285), G139 (= G286), S140 (= S287), L143 (≠ S290)
- binding glutamine: G89 (= G242), T137 (= T284), G138 (≠ L285), S140 (= S287), Y168 (≠ L315), Y271 (≠ T414), Y272 (≠ I415)
Sites not aligning to the query:
9fz1A umg-sp3 (see paper)
30% identity, 39% coverage: 119:337/555 of query aligns to 4:229/438 of 9fz1A
Sites not aligning to the query:
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
26% identity, 73% coverage: 135:540/555 of query aligns to 19:441/461 of 4gysB
- active site: K72 (= K191), S146 (= S263), S147 (= S264), T165 (= T282), T167 (= T284), A168 (≠ L285), G169 (= G286), S170 (= S287), V173 (≠ S290)
- binding malonate ion: A120 (= A240), G122 (= G242), S146 (= S263), T167 (= T284), A168 (≠ L285), S170 (= S287), S193 (≠ Y310), G194 (= G311), V195 (≠ A312), R200 (≠ W317), Y297 (vs. gap), R305 (≠ E418)
Query Sequence
>WP_101444719.1 NCBI__GCF_002846395.1:WP_101444719.1
MKKSYTYTALGAICFLSGAFVMKLADDKITVDMLRSAQQMIGLNFTDAQLDSATTSVAEF
REGYQRIRKQPLANEVTPALQFNPIPVGFEFEQKREKFEVERRKGIKLPTNREELAFYSV
PQLAELVRTKQISSEELTKFFLDRLKQHGPTLQCVTSLTEELALEQARRADQEIKAGKYK
GMLHGIPYGVKDLLATKKYKTTWGSVPYKDQQIDLDATVVERLEQAGAVLVAKLTLGELA
MGDVWYGGKTRSPWDTTKGSSGSSAGSASAVSAGLLPFAIGTETLGSIVSPSTACGTTGL
RPTYGRVSRYGAMALSWSMDKIGPIARSAEDCAIVFNAIYGPDGKDLTVANAPFNYNKSI
EAKKLRVGYLHKDFERDYPFKENDKATLEALRKAGIELVPIELPNLPARDLTLTISVEGA
AAFDELTRSGRDSLMVQQHKNAWPNIFRAGRFVTAVEYLQAQRVRSLIIQQMHEQLKGID
VYLSPSFAGSNLVMTNLSGHPCVVVPNGFQKNGMPTTITFMGQLYGEAKVLALAKLYQDL
TNHDEQRPPMALSSR
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