SitesBLAST
Comparing WP_012331585.1 NCBI__GCF_000019365.1:WP_012331585.1 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)
3kfuE Crystal structure of the transamidosome (see paper)
38% identity, 95% coverage: 15:468/480 of query aligns to 1:457/468 of 3kfuE
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 94% coverage: 13:465/480 of query aligns to 8:466/478 of 3h0mA
- active site: K72 (= K84), S147 (= S159), S148 (= S160), S166 (= S178), T168 (≠ H180), G169 (≠ A181), G170 (= G182), S171 (= S183), Q174 (≠ N186)
- binding glutamine: M122 (≠ L134), G123 (= G135), D167 (= D179), T168 (≠ H180), G169 (≠ A181), G170 (= G182), S171 (= S183), F199 (= F211), Y302 (≠ W316), R351 (vs. gap), D418 (≠ W415)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 94% coverage: 13:465/480 of query aligns to 8:466/478 of 3h0lA
- active site: K72 (= K84), S147 (= S159), S148 (= S160), S166 (= S178), T168 (≠ H180), G169 (≠ A181), G170 (= G182), S171 (= S183), Q174 (≠ N186)
- binding asparagine: G123 (= G135), S147 (= S159), G169 (≠ A181), G170 (= G182), S171 (= S183), Y302 (≠ W316), R351 (vs. gap), D418 (≠ W415)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
38% identity, 48% coverage: 12:241/480 of query aligns to 7:240/457 of 5h6sC
- active site: K77 (= K84), S152 (= S159), S153 (= S160), L173 (≠ H180), G174 (≠ A181), G175 (= G182), S176 (= S183)
- binding 4-oxidanylbenzohydrazide: C126 (≠ G133), R128 (≠ G135), W129 (≠ S136), S152 (= S159), L173 (≠ H180), G174 (≠ A181), S176 (= S183)
Sites not aligning to the query:
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
26% identity, 94% coverage: 14:466/480 of query aligns to 10:474/485 of 2f2aA
- active site: K79 (= K84), S154 (= S159), S155 (= S160), S173 (= S178), T175 (≠ H180), G176 (≠ A181), G177 (= G182), S178 (= S183), Q181 (≠ N186)
- binding glutamine: G130 (= G135), S154 (= S159), D174 (= D179), T175 (≠ H180), G176 (≠ A181), S178 (= S183), F206 (= F211), Y309 (≠ W316), Y310 (≠ R317), R358 (= R352), D425 (≠ W415)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
26% identity, 94% coverage: 14:466/480 of query aligns to 10:474/485 of 2dqnA
- active site: K79 (= K84), S154 (= S159), S155 (= S160), S173 (= S178), T175 (≠ H180), G176 (≠ A181), G177 (= G182), S178 (= S183), Q181 (≠ N186)
- binding asparagine: M129 (≠ L134), G130 (= G135), T175 (≠ H180), G176 (≠ A181), S178 (= S183), Y309 (≠ W316), Y310 (≠ R317), R358 (= R352), D425 (≠ W415)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
30% identity, 95% coverage: 12:468/480 of query aligns to 8:476/490 of 4yjiA
- active site: K79 (= K84), S158 (= S159), S159 (= S160), G179 (≠ H180), G180 (≠ A181), G181 (= G182), A182 (≠ S183)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ T86), G132 (= G133), S158 (= S159), G179 (≠ H180), G180 (≠ A181), A182 (≠ S183)
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
27% identity, 97% coverage: 2:465/480 of query aligns to 117:588/607 of Q7XJJ7
- K205 (= K84) mutation to A: Loss of activity.
- SS 281:282 (= SS 159:160) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ HAGS 180:183) binding substrate
- S305 (= S183) mutation to A: Loss of activity.
- R307 (= R185) mutation to A: Loss of activity.
- S360 (≠ P238) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
27% identity, 97% coverage: 2:465/480 of query aligns to 117:588/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (= G133), T258 (≠ S136), S281 (= S159), G302 (≠ H180), G303 (≠ A181), S305 (= S183), S472 (≠ E348), I532 (≠ M409), M539 (= M416)
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
27% identity, 97% coverage: 2:465/480 of query aligns to 117:588/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (= G133), G302 (≠ H180), G303 (≠ A181), G304 (= G182), A305 (≠ S183), V442 (= V318), I475 (≠ E351), M539 (= M416)
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, 97% coverage: 2:465/480 of query aligns to 117:588/605 of 8ey1D
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
29% identity, 95% coverage: 13:469/480 of query aligns to 31:491/507 of Q84DC4
- T31 (= T13) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K84) mutation to A: Abolishes activity on mandelamide.
- S180 (= S159) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S160) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ A181) 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 (= S183) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ N186) 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 (≠ V312) 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 (≠ D376) 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 (≠ M416) 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.
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
31% identity, 91% coverage: 11:449/480 of query aligns to 2:432/457 of 6c6gA
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
32% identity, 93% coverage: 24:468/480 of query aligns to 20:479/487 of 1m21A
- active site: K81 (= K84), S160 (= S159), S161 (= S160), T179 (≠ S178), T181 (≠ H180), D182 (≠ A181), G183 (= G182), S184 (= S183), C187 (≠ N186)
- binding : A129 (≠ G133), N130 (vs. gap), F131 (vs. gap), C158 (≠ G157), G159 (= G158), S160 (= S159), S184 (= S183), C187 (≠ N186), I212 (≠ F211), R318 (= R317), L321 (≠ R320), L365 (≠ A345), F426 (vs. gap)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
37% identity, 48% coverage: 12:240/480 of query aligns to 7:231/482 of 3a2qA
- active site: K69 (= K84), S147 (= S159), S148 (= S160), N166 (≠ S178), A168 (≠ H180), A169 (= A181), G170 (= G182), A171 (≠ S183), I174 (≠ N186)
- binding 6-aminohexanoic acid: G121 (= G133), G121 (= G133), N122 (≠ L134), S147 (= S159), A168 (≠ H180), A168 (≠ H180), A169 (= A181), A171 (≠ S183)
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)
36% identity, 47% coverage: 14:240/480 of query aligns to 9:241/564 of 6te4A
Sites not aligning to the query:
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
29% identity, 91% coverage: 25:461/480 of query aligns to 17:434/461 of 4gysB
- active site: K72 (= K84), S146 (= S159), S147 (= S160), T165 (≠ S178), T167 (≠ H180), A168 (= A181), G169 (= G182), S170 (= S183), V173 (≠ N186)
- binding malonate ion: A120 (≠ G133), G122 (= G135), S146 (= S159), T167 (≠ H180), A168 (= A181), S170 (= S183), S193 (≠ R206), G194 (≠ T207), V195 (≠ D208), R200 (≠ P213), Y297 (≠ R314), R305 (= R320)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
29% identity, 83% coverage: 74:469/480 of query aligns to 85:501/508 of 3a1iA
- active site: K95 (= K84), S170 (= S159), S171 (= S160), G189 (≠ S178), Q191 (≠ H180), G192 (≠ A181), G193 (= G182), A194 (≠ S183), I197 (≠ N186)
- binding benzamide: F145 (≠ L134), S146 (≠ G135), G147 (≠ S136), Q191 (≠ H180), G192 (≠ A181), G193 (= G182), A194 (≠ S183), W327 (= W316)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
45% identity, 26% coverage: 75:201/480 of query aligns to 82:207/605 of Q936X2
- K91 (= K84) mutation to A: Loss of activity.
- S165 (= S159) mutation to A: Loss of activity.
- S189 (= S183) mutation to A: Loss of activity.
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
28% identity, 81% coverage: 74:461/480 of query aligns to 52:403/412 of 1o9oA
- active site: K62 (= K84), A131 (≠ S159), S132 (= S160), T150 (≠ S178), T152 (≠ H180), G153 (≠ A181), G154 (= G182), S155 (= S183), R158 (≠ N186)
- binding 3-amino-3-oxopropanoic acid: G130 (= G158), T152 (≠ H180), G153 (≠ A181), G154 (= G182), S155 (= S183), R158 (≠ N186), P359 (≠ D410)
Query Sequence
>WP_012331585.1 NCBI__GCF_000019365.1:WP_012331585.1
MSLSPDLVSSRATDLARAIRDRTVSAREVMRAHLDRIARANPAANAIVGLRDPEILLEEA
ACADRDLAAGRWRGPLHGLPHAVKDTSPAAGLIWTQGSPLFAGRVAEADAPHVARLRQAG
AILIGKTNVPEFGLGSHTVNPVFGATRNAYDPARSAGGSSGGAAVALALRMLPLADGSDH
AGSLRNPAAWNGVLGLRPSPGRVPMRTDEVFLPDLTVAGPMARCTADLGLLLSVLAGPDP
RLPHSLTEDPSAFAAPAPLALAGLRIGWLGDLGGHLPVEPGILALCERALAVFAGEGARV
APLALGFDAEAVFRAWRVLRAWQAGAALAPHARDPAARAALKPDALFEIDERARLDAYAV
QAASALRSRWFAHLLDLFARCDLLALPAAQVFPFPIGEMWPRAIAGRPMDSYHRWMEVAI
PATMGGCPAISLPAGRGPGGLPMGLQLIAPHRGEGRLLAVAAAYEAATGFDREAPAITAL
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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