SitesBLAST
Comparing WP_028489611.1 NCBI__GCF_000621325.1:WP_028489611.1 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)
51% identity, 98% coverage: 5:482/486 of query aligns to 6:476/478 of 3h0mA
- active site: K72 (= K77), S147 (= S152), S148 (= S153), S166 (≠ T171), T168 (= T173), G169 (= G174), G170 (= G175), S171 (= S176), Q174 (= Q179)
- binding glutamine: M122 (= M127), G123 (= G128), D167 (= D172), T168 (= T173), G169 (= G174), G170 (= G175), S171 (= S176), F199 (= F204), Y302 (= Y307), R351 (= R356), D418 (= D423)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
51% identity, 98% coverage: 5:482/486 of query aligns to 6:476/478 of 3h0lA
- active site: K72 (= K77), S147 (= S152), S148 (= S153), S166 (≠ T171), T168 (= T173), G169 (= G174), G170 (= G175), S171 (= S176), Q174 (= Q179)
- binding asparagine: G123 (= G128), S147 (= S152), G169 (= G174), G170 (= G175), S171 (= S176), Y302 (= Y307), R351 (= R356), D418 (= D423)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
48% identity, 93% coverage: 29:478/486 of query aligns to 31:479/485 of 2f2aA
- active site: K79 (= K77), S154 (= S152), S155 (= S153), S173 (≠ T171), T175 (= T173), G176 (= G174), G177 (= G175), S178 (= S176), Q181 (= Q179)
- binding glutamine: G130 (= G128), S154 (= S152), D174 (= D172), T175 (= T173), G176 (= G174), S178 (= S176), F206 (= F204), Y309 (= Y307), Y310 (= Y308), R358 (= R356), D425 (= D423)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
48% identity, 93% coverage: 29:478/486 of query aligns to 31:479/485 of 2dqnA
- active site: K79 (= K77), S154 (= S152), S155 (= S153), S173 (≠ T171), T175 (= T173), G176 (= G174), G177 (= G175), S178 (= S176), Q181 (= Q179)
- binding asparagine: M129 (= M127), G130 (= G128), T175 (= T173), G176 (= G174), S178 (= S176), Y309 (= Y307), Y310 (= Y308), R358 (= R356), D425 (= D423)
3kfuE Crystal structure of the transamidosome (see paper)
45% identity, 98% coverage: 9:482/486 of query aligns to 5:465/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
32% identity, 91% coverage: 28:470/486 of query aligns to 6:448/450 of 4n0iA
- active site: K38 (= K77), S116 (= S152), S117 (= S153), T135 (= T171), T137 (= T173), G138 (= G174), G139 (= G175), S140 (= S176), L143 (≠ Q179)
- binding glutamine: G89 (= G128), T137 (= T173), G138 (= G174), S140 (= S176), Y168 (≠ F204), Y271 (= Y307), Y272 (= Y308), R320 (= R356), D404 (= D423)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
33% identity, 95% coverage: 9:472/486 of query aligns to 6:448/457 of 6c6gA
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
32% identity, 95% coverage: 16:475/486 of query aligns to 18:479/487 of 1m21A
- active site: K81 (= K77), S160 (= S152), S161 (= S153), T179 (= T171), T181 (= T173), D182 (≠ G174), G183 (= G175), S184 (= S176), C187 (≠ Q179)
- binding : A129 (= A126), N130 (≠ M127), F131 (≠ G128), C158 (≠ G150), G159 (= G151), S160 (= S152), S184 (= S176), C187 (≠ Q179), I212 (≠ F204), R318 (≠ Y308), L321 (≠ A311), L365 (≠ I357), F426 (≠ Y420)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
31% identity, 84% coverage: 67:473/486 of query aligns to 85:498/508 of 3a1iA
- active site: K95 (= K77), S170 (= S152), S171 (= S153), G189 (≠ T171), Q191 (≠ T173), G192 (= G174), G193 (= G175), A194 (≠ S176), I197 (≠ Q179)
- binding benzamide: F145 (≠ M127), S146 (≠ G128), G147 (≠ S129), Q191 (≠ T173), G192 (= G174), G193 (= G175), A194 (≠ S176), W327 (≠ Y307)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
30% identity, 94% coverage: 13:469/486 of query aligns to 37:484/507 of Q84DC4
- K100 (= K77) mutation to A: Abolishes activity on mandelamide.
- S180 (= S152) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S153) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G174) 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 (= S176) mutation to A: Abolishes activity on mandelamide.
- Q207 (= Q179) 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 (≠ A303) 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 (≠ D370) 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.
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.
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, 79% coverage: 102:485/486 of query aligns to 231:600/607 of Q7XJJ7
- SS 281:282 (= SS 152:153) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 173:176) binding
- S305 (= S176) mutation to A: Loss of activity.
- R307 (= R178) mutation to A: Loss of activity.
- S360 (≠ L231) mutation to A: No effect.
Sites not aligning to the query:
- 205 K→A: Loss of activity.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
30% identity, 79% coverage: 102:485/486 of query aligns to 231:600/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A126), T258 (≠ S129), S281 (= S152), G302 (≠ T173), G303 (= G174), S305 (= S176), S472 (≠ T361), I532 (≠ S418), M539 (vs. gap)
Sites not aligning to the query:
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
28% identity, 97% coverage: 4:473/486 of query aligns to 5:445/457 of 5h6sC
- active site: K77 (= K77), S152 (= S152), S153 (= S153), L173 (≠ T173), G174 (= G174), G175 (= G175), S176 (= S176)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A126), R128 (≠ G128), W129 (≠ S129), S152 (= S152), L173 (≠ T173), G174 (= G174), S176 (= S176), W306 (≠ Y307), F338 (≠ I359)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
29% identity, 97% coverage: 13:482/486 of query aligns to 14:478/482 of 3a2qA
- active site: K69 (= K77), S147 (= S152), S148 (= S153), N166 (≠ T171), A168 (≠ T173), A169 (≠ G174), G170 (= G175), A171 (≠ S176), I174 (≠ Q179)
- binding 6-aminohexanoic acid: G121 (≠ A126), G121 (≠ A126), N122 (≠ M127), S147 (= S152), A168 (≠ T173), A168 (≠ T173), A169 (≠ G174), A171 (≠ S176), C313 (= C315)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
26% identity, 99% coverage: 1:483/486 of query aligns to 3:486/490 of 4yjiA
- active site: K79 (= K77), S158 (= S152), S159 (= S153), G179 (≠ T173), G180 (= G174), G181 (= G175), A182 (≠ S176)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L79), G132 (≠ A126), S158 (= S152), G179 (≠ T173), G180 (= G174), A182 (≠ S176)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
30% identity, 97% coverage: 3:473/486 of query aligns to 2:439/461 of 4gysB
- active site: K72 (= K77), S146 (= S152), S147 (= S153), T165 (= T171), T167 (= T173), A168 (≠ G174), G169 (= G175), S170 (= S176), V173 (≠ Q179)
- binding malonate ion: A120 (= A126), G122 (= G128), S146 (= S152), T167 (= T173), A168 (≠ G174), S170 (= S176), S193 (≠ Y199), G194 (= G200), V195 (≠ M201), R200 (≠ S206), Y297 (≠ F322), R305 (= R330)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
26% identity, 88% coverage: 47:473/486 of query aligns to 62:462/605 of Q936X2
- K91 (= K77) mutation to A: Loss of activity.
- S165 (= S152) mutation to A: Loss of activity.
- S189 (= S176) mutation to A: Loss of activity.
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
25% identity, 96% coverage: 4:468/486 of query aligns to 2:403/412 of 1o9oA
- active site: K62 (= K77), A131 (≠ S152), S132 (= S153), T150 (= T171), T152 (= T173), G153 (= G174), G154 (= G175), S155 (= S176), R158 (≠ Q179)
- binding 3-amino-3-oxopropanoic acid: G130 (= G151), T152 (= T173), G153 (= G174), G154 (= G175), S155 (= S176), R158 (≠ Q179), P359 (= P416)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
25% identity, 96% coverage: 4:468/486 of query aligns to 2:403/412 of 1ocmA
- active site: K62 (= K77), S131 (= S152), S132 (= S153), T152 (= T173), G153 (= G174), G154 (= G175), S155 (= S176)
- binding pyrophosphate 2-: R113 (≠ S130), S131 (= S152), Q151 (≠ D172), T152 (= T173), G153 (= G174), G154 (= G175), S155 (= S176), R158 (≠ Q179), P359 (≠ D423)
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)
34% identity, 44% coverage: 4:219/486 of query aligns to 77:288/579 of Q9TUI8
- S217 (= S152) mutation to A: Loss of activity.
- S218 (= S153) mutation to A: Lowers activity by at least 98%.
- D237 (= D172) mutation D->E,N: Loss of activity.
- S241 (= S176) mutation to A: Loss of activity.
- C249 (= C184) mutation to A: Loss of activity.
Query Sequence
>WP_028489611.1 NCBI__GCF_000621325.1:WP_028489611.1
MHTLSLKGIHDGVHTGKFSVMEATDAYLDRIERFNPELNAYITVTRDTAKTQAVDIDNRI
RKGELTGAMAGVPYALKDLFCSEGVLTTCASNMLANFISPYDAHVAEKLKAAGGVLLGKN
NMDEFAMGSSNETSAFGSVCNPWDVSKVPGGSSGGGAATIAARLAPMTLGTDTGGSIRQP
ASFCNITGIKPTYGRISRYGMIAFASSLDQCGPMAASAEDCALTLNIIAGLDGRDSTCMD
LPVPDYTATLNGSLEGLRIGLPKEFFAEGLDAQVADVIDRAIKQFQAKGAIIKEVTLPNS
HLAVPVYYVVAPAECSSNLSRFDGVRFGHRCENPKDLMDLYERSRWEGFGDEVKRRIMIG
TYALSAGYYDAYYLKAQQVRRLIKQDFEAAFKDVDVIMGPSCPTTAFGIGEKKDDPISMY
LEDLYTIPVSLAGLPGMTFPIGFAADGLPVGMQLVGNYFEEARMLNIAHQYQQWTDWHTQ
VPARFA
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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