SitesBLAST
Comparing WP_011384077.1 NCBI__GCF_000009985.1:WP_011384077.1 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)
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)
35% identity, 92% coverage: 24:383/391 of query aligns to 28:416/425 of Q9FR37
- K36 (= K32) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S109) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S110) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D129) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S133) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C141) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (vs. gap) mutation to T: Slightly reduces catalytic activity.
Q9MUK5 Translocon at the outer membrane of chloroplasts 64 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
33% identity, 92% coverage: 25:382/391 of query aligns to 62:444/593 of Q9MUK5
Sites not aligning to the query:
- 516 N→A: Loss of HSP90 binding, but no effect on HSP70 binding.
- 550 R→A: 80% decrease of HSP70 and HSP90 binding.
3kfuE Crystal structure of the transamidosome (see paper)
32% identity, 93% coverage: 23:385/391 of query aligns to 56:450/468 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)
28% identity, 93% coverage: 24:385/391 of query aligns to 197:584/607 of Q7XJJ7
- K205 (= K32) mutation to A: Loss of activity.
- SS 281:282 (= SS 109:110) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TAGS 130:133) binding
- S305 (= S133) mutation to A: Loss of activity.
- R307 (= R135) mutation to A: Loss of activity.
- S360 (vs. gap) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
28% identity, 93% coverage: 24:385/391 of query aligns to 197:584/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ T83), T258 (≠ I86), S281 (= S109), G302 (≠ T130), G303 (≠ A131), S305 (= S133), S472 (≠ G272), I532 (≠ W334), M539 (≠ V341)
Sites not aligning to the query:
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
31% identity, 96% coverage: 13:388/391 of query aligns to 80:486/507 of Q84DC4
- K100 (= K32) mutation to A: Abolishes activity on mandelamide.
- S180 (= S109) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S110) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ A131) 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 (= S133) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ V136) 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 (≠ Q248) 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 (= Q287) 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 (≠ V341) 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.
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 92% coverage: 23:382/391 of query aligns to 63:459/478 of 3h0mA
- active site: K72 (= K32), S147 (= S109), S148 (= S110), S166 (≠ T128), T168 (= T130), G169 (≠ A131), G170 (= G132), S171 (= S133), Q174 (≠ V136)
- binding glutamine: M122 (≠ R84), G123 (= G85), D167 (= D129), T168 (= T130), G169 (≠ A131), G170 (= G132), S171 (= S133), F199 (≠ Q161), Y302 (vs. gap), R351 (≠ N278), D418 (≠ S342)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 92% coverage: 23:382/391 of query aligns to 63:459/478 of 3h0lA
- active site: K72 (= K32), S147 (= S109), S148 (= S110), S166 (≠ T128), T168 (= T130), G169 (≠ A131), G170 (= G132), S171 (= S133), Q174 (≠ V136)
- binding asparagine: G123 (= G85), S147 (= S109), G169 (≠ A131), G170 (= G132), S171 (= S133), Y302 (vs. gap), R351 (≠ N278), D418 (≠ S342)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
44% identity, 42% coverage: 23:185/391 of query aligns to 65:226/457 of 6c6gA
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
30% identity, 94% coverage: 23:390/391 of query aligns to 63:439/461 of 4gysB
- active site: K72 (= K32), S146 (= S109), S147 (= S110), T165 (= T128), T167 (= T130), A168 (= A131), G169 (= G132), S170 (= S133), V173 (= V136)
- binding malonate ion: A120 (≠ T83), G122 (= G85), S146 (= S109), T167 (= T130), A168 (= A131), S170 (= S133), S193 (≠ D156), G194 (= G157), V195 (= V158), R200 (≠ N163), Y297 (≠ Q252), R305 (≠ A256)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
28% identity, 93% coverage: 23:385/391 of query aligns to 72:472/487 of 1m21A
- active site: K81 (= K32), S160 (= S109), S161 (= S110), T179 (= T128), T181 (= T130), D182 (≠ A131), G183 (= G132), S184 (= S133), C187 (≠ V136)
- binding : A129 (≠ T83), N130 (vs. gap), F131 (vs. gap), C158 (≠ G107), G159 (= G108), S160 (= S109), S184 (= S133), C187 (≠ V136), I212 (≠ Q161), R318 (≠ N249), L321 (≠ Q252), L365 (≠ N278), F426 (≠ L343)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
32% identity, 93% coverage: 21:385/391 of query aligns to 51:403/412 of 1o9oA
- active site: K62 (= K32), A131 (≠ S109), S132 (= S110), T150 (= T128), T152 (= T130), G153 (≠ A131), G154 (= G132), S155 (= S133), R158 (≠ V136)
- binding 3-amino-3-oxopropanoic acid: G130 (= G108), T152 (= T130), G153 (≠ A131), G154 (= G132), S155 (= S133), R158 (≠ V136), P359 (≠ H338)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
32% identity, 93% coverage: 21:385/391 of query aligns to 51:403/412 of 1ocmA
- active site: K62 (= K32), S131 (= S109), S132 (= S110), T152 (= T130), G153 (≠ A131), G154 (= G132), S155 (= S133)
- binding pyrophosphate 2-: R113 (≠ N90), S131 (= S109), Q151 (≠ D129), T152 (= T130), G153 (≠ A131), G154 (= G132), S155 (= S133), R158 (≠ V136), P359 (≠ H338)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
27% identity, 84% coverage: 58:386/391 of query aligns to 103:471/485 of 2f2aA
- active site: S154 (= S109), S155 (= S110), S173 (≠ T128), T175 (= T130), G176 (≠ A131), G177 (= G132), S178 (= S133), Q181 (≠ V136)
- binding glutamine: G130 (= G85), S154 (= S109), D174 (= D129), T175 (= T130), G176 (≠ A131), S178 (= S133), F206 (≠ Q161), Y309 (vs. gap), Y310 (vs. gap), R358 (≠ N278), D425 (≠ I336)
Sites not aligning to the query:
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
27% identity, 84% coverage: 58:386/391 of query aligns to 103:471/485 of 2dqnA
- active site: S154 (= S109), S155 (= S110), S173 (≠ T128), T175 (= T130), G176 (≠ A131), G177 (= G132), S178 (= S133), Q181 (≠ V136)
- binding asparagine: M129 (≠ R84), G130 (= G85), T175 (= T130), G176 (≠ A131), S178 (= S133), Y309 (vs. gap), Y310 (vs. gap), R358 (≠ N278), D425 (≠ I336)
Sites not aligning to the query:
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
40% identity, 41% coverage: 20:181/391 of query aligns to 79:240/605 of Q936X2
- K91 (= K32) mutation to A: Loss of activity.
- S165 (= S109) mutation to A: Loss of activity.
- S189 (= S133) mutation to A: Loss of activity.
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
25% identity, 98% coverage: 5:388/391 of query aligns to 9:449/450 of 4n0iA
- active site: K38 (= K32), S116 (= S109), S117 (= S110), T135 (= T128), T137 (= T130), G138 (≠ A131), G139 (= G132), S140 (= S133), L143 (≠ V136)
- binding glutamine: G89 (= G85), T137 (= T130), G138 (≠ A131), S140 (= S133), Y168 (≠ Q161), Y271 (≠ V231), Y272 (≠ R234), R320 (vs. gap), D404 (≠ E335)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
38% identity, 34% coverage: 22:154/391 of query aligns to 67:197/457 of 5h6sC
- active site: K77 (= K32), S152 (= S109), S153 (= S110), L173 (≠ T130), G174 (≠ A131), G175 (= G132), S176 (= S133)
- binding 4-oxidanylbenzohydrazide: C126 (≠ T83), R128 (≠ G85), W129 (≠ I86), S152 (= S109), L173 (≠ T130), G174 (≠ A131), S176 (= S133)
Sites not aligning to the query:
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
38% identity, 34% coverage: 21:153/391 of query aligns to 58:191/482 of 3a2qA
- active site: K69 (= K32), S147 (= S109), S148 (= S110), N166 (≠ T128), A168 (≠ T130), A169 (= A131), G170 (= G132), A171 (≠ S133), I174 (≠ V136)
- binding 6-aminohexanoic acid: G121 (≠ T83), G121 (≠ T83), N122 (≠ R84), S147 (= S109), A168 (≠ T130), A168 (≠ T130), A169 (= A131), A171 (≠ S133)
Sites not aligning to the query:
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
34% identity, 49% coverage: 22:212/391 of query aligns to 85:273/508 of 3a1iA
- active site: K95 (= K32), S170 (= S109), S171 (= S110), G189 (≠ T128), Q191 (≠ T130), G192 (≠ A131), G193 (= G132), A194 (≠ S133), I197 (≠ V136)
- binding benzamide: F145 (≠ R84), S146 (≠ G85), G147 (≠ I86), Q191 (≠ T130), G192 (≠ A131), G193 (= G132), A194 (≠ S133)
Sites not aligning to the query:
Query Sequence
>WP_011384077.1 NCBI__GCF_000009985.1:WP_011384077.1
MHDPLNAFALGGDVYLNGAETGPLAGLTFAAKDVFDVAGYVTGAGNPDWRRLAEPAKHTA
WAIGTLLESGARLVGKTHTDELTRGIFGDNSHYGTPDNPRAPGHVPGGSSSGSAAAVAGG
LCSMALGTDTAGSTRVPASFCGVFGLRPTLGTIPMDGVLSQSNTFDTVGLLADDPEILAK
MGEALLRKKIKDTRPAQVVVLEDALEASDPAVAAAIEAALPRIKEAVAPIVRGRKLSPVP
LADWVEHQNAIQGREAWETFGEWINNSNPRFGFEVADNFLRGSKVSQRTLSAARGFRLRA
KRWVQEALEGNAMLVLPTTPVTAPPVHSPRSVMWEIRHRIVSLTTIAGMAGCPQISLPLC
KVDGLPVGLSLIGPRGSDALLLAAAQRIGKA
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