SitesBLAST
Comparing WP_014450045.1 NCBI__GCF_000284315.1:WP_014450045.1 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, 95% coverage: 13:480/493 of query aligns to 6:467/478 of 3h0mA
- active site: K72 (= K84), S147 (= S159), S148 (= S160), S166 (= S178), T168 (= T180), G169 (= G181), G170 (= G182), S171 (= S183), Q174 (= Q186)
- binding glutamine: M122 (= M134), G123 (= G135), D167 (= D179), T168 (= T180), G169 (= G181), G170 (= G182), S171 (= S183), F199 (= F211), Y302 (= Y314), R351 (= R363), D418 (= D430)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
51% identity, 95% coverage: 13:480/493 of query aligns to 6:467/478 of 3h0lA
- active site: K72 (= K84), S147 (= S159), S148 (= S160), S166 (= S178), T168 (= T180), G169 (= G181), G170 (= G182), S171 (= S183), Q174 (= Q186)
- binding asparagine: G123 (= G135), S147 (= S159), G169 (= G181), G170 (= G182), S171 (= S183), Y302 (= Y314), R351 (= R363), D418 (= D430)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
50% identity, 90% coverage: 30:475/493 of query aligns to 24:469/485 of 2f2aA
- active site: K79 (= K84), S154 (= S159), S155 (= S160), S173 (= S178), T175 (= T180), G176 (= G181), G177 (= G182), S178 (= S183), Q181 (= Q186)
- binding glutamine: G130 (= G135), S154 (= S159), D174 (= D179), T175 (= T180), G176 (= G181), S178 (= S183), F206 (= F211), Y309 (= Y314), Y310 (= Y315), R358 (= R363), D425 (= D430)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
50% identity, 90% coverage: 30:475/493 of query aligns to 24:469/485 of 2dqnA
- active site: K79 (= K84), S154 (= S159), S155 (= S160), S173 (= S178), T175 (= T180), G176 (= G181), G177 (= G182), S178 (= S183), Q181 (= Q186)
- binding asparagine: M129 (= M134), G130 (= G135), T175 (= T180), G176 (= G181), S178 (= S183), Y309 (= Y314), Y310 (= Y315), R358 (= R363), D425 (= D430)
3kfuE Crystal structure of the transamidosome (see paper)
47% identity, 94% coverage: 19:480/493 of query aligns to 6:455/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
36% identity, 89% coverage: 36:472/493 of query aligns to 6:443/450 of 4n0iA
- active site: K38 (= K84), S116 (= S159), S117 (= S160), T135 (≠ S178), T137 (= T180), G138 (= G181), G139 (= G182), S140 (= S183), L143 (≠ Q186)
- binding glutamine: G89 (= G135), T137 (= T180), G138 (= G181), S140 (= S183), Y168 (≠ F211), Y271 (= Y314), Y272 (= Y315), R320 (= R363), D404 (= D430)
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: 24:480/493 of query aligns to 13:449/457 of 6c6gA
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
31% identity, 94% coverage: 12:475/493 of query aligns to 6:472/487 of 1m21A
- active site: K81 (= K84), S160 (= S159), S161 (= S160), T179 (≠ S178), T181 (= T180), D182 (≠ G181), G183 (= G182), S184 (= S183), C187 (≠ Q186)
- binding : A129 (= A133), N130 (≠ M134), F131 (≠ G135), C158 (≠ G157), G159 (= G158), S160 (= S159), S184 (= S183), C187 (≠ Q186), I212 (≠ F211), R318 (≠ Y315), L321 (≠ A318), L365 (= L365), F426 (≠ Y427)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
31% identity, 81% coverage: 75:473/493 of query aligns to 86:491/508 of 3a1iA
- active site: K95 (= K84), S170 (= S159), S171 (= S160), G189 (≠ S178), Q191 (≠ T180), G192 (= G181), G193 (= G182), A194 (≠ S183), I197 (≠ Q186)
- binding benzamide: F145 (≠ M134), S146 (≠ G135), G147 (≠ S136), Q191 (≠ T180), G192 (= G181), G193 (= G182), A194 (≠ S183), W327 (≠ Y314)
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, 84% coverage: 66:480/493 of query aligns to 179:589/607 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 (≠ TGGS 180:183) binding
- S305 (= S183) mutation to A: Loss of activity.
- R307 (= R185) mutation to A: Loss of activity.
- S360 (≠ H238) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
28% identity, 84% coverage: 66:480/493 of query aligns to 179:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A133), T258 (≠ S136), S281 (= S159), G302 (≠ T180), G303 (= G181), S305 (= S183), S472 (≠ T368), I532 (≠ S421), M539 (≠ L428)
Sites not aligning to the query:
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
27% identity, 95% coverage: 26:492/493 of query aligns to 42:500/507 of Q84DC4
- 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 (= G181) 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 (= Q186) 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 (≠ A310) 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 (≠ F369) 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 (≠ S435) 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.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
31% identity, 93% coverage: 27:485/493 of query aligns to 17:444/461 of 4gysB
- active site: K72 (= K84), S146 (= S159), S147 (= S160), T165 (≠ S178), T167 (= T180), A168 (≠ G181), G169 (= G182), S170 (= S183), V173 (≠ Q186)
- binding malonate ion: A120 (= A133), G122 (= G135), S146 (= S159), T167 (= T180), A168 (≠ G181), S170 (= S183), S193 (≠ Q206), G194 (= G207), V195 (≠ L208), R200 (≠ S213), Y297 (= Y315), R305 (= R337)
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)
30% identity, 80% coverage: 78:472/493 of query aligns to 30:415/425 of Q9FR37
- K36 (= K84) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S159) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S160) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D179) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S183) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C191) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (= S245) mutation to T: Slightly reduces catalytic activity.
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
28% identity, 92% coverage: 19:474/493 of query aligns to 11:439/457 of 5h6sC
- active site: K77 (= K84), S152 (= S159), S153 (= S160), L173 (≠ T180), G174 (= G181), G175 (= G182), S176 (= S183)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A133), R128 (≠ G135), W129 (≠ S136), S152 (= S159), L173 (≠ T180), G174 (= G181), S176 (= S183), W306 (≠ Y314), F338 (= F369)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
30% identity, 89% coverage: 42:480/493 of query aligns to 48:464/605 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.
Q9MUK5 Translocon at the outer membrane of chloroplasts 64 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
45% identity, 29% coverage: 81:225/493 of query aligns to 66:212/593 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.
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
34% identity, 48% coverage: 6:242/493 of query aligns to 2:233/482 of 3a2qA
- active site: K69 (= K84), S147 (= S159), S148 (= S160), N166 (≠ S178), A168 (≠ T180), A169 (≠ G181), G170 (= G182), A171 (≠ S183), I174 (≠ Q186)
- binding 6-aminohexanoic acid: G121 (≠ A133), G121 (≠ A133), N122 (≠ M134), S147 (= S159), A168 (≠ T180), A168 (≠ T180), A169 (≠ G181), A171 (≠ S183)
Sites not aligning to the query:
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
24% identity, 92% coverage: 11:463/493 of query aligns to 1:391/412 of 1ocmA
- active site: K62 (= K84), S131 (= S159), S132 (= S160), T152 (= T180), G153 (= G181), G154 (= G182), S155 (= S183)
- binding pyrophosphate 2-: R113 (≠ G135), S131 (= S159), Q151 (≠ D179), T152 (= T180), G153 (= G181), G154 (= G182), S155 (= S183), R158 (≠ Q186), P359 (= P423)
4do3A Structure of faah with a non-steroidal anti-inflammatory drug (see paper)
31% identity, 54% coverage: 46:313/493 of query aligns to 69:342/543 of 4do3A
- active site: K110 (= K84), S185 (= S159), S186 (= S160), T204 (≠ S178), I206 (≠ T180), G207 (= G181), G208 (= G182), S209 (= S183), F212 (≠ Q186)
- binding (2S)-2-(6-chloro-9H-carbazol-2-yl)propanoic acid: L160 (≠ M134)
- binding cyclohexane aminocarboxylic acid: L160 (≠ M134), I206 (≠ T180), G207 (= G181), S209 (= S183)
Sites not aligning to the query:
Query Sequence
>WP_014450045.1 NCBI__GCF_000284315.1:WP_014450045.1
MGKTQDIGKLLSSVADFARARDEGSVTIEEVTEFCLSRIDSRDGKLGAFLTINPNAKNRA
RQLDNRRSELSKRSLFYGYPIAIKDNLNIEGLPTTCASRILANHRSIYTATAVSRLLSAG
AVVLGKTNMDEFAMGSSTENSAMGITRNPWDHDRVPGGSSGGSAVAVSGGMAPMSLGSDT
GGSIRQPAAFCGVLGLKPTYGRISRQGLVAFSSSLDQIGPFAQNPLDALHVTVLLSGHDP
LDMTSSTRDPLEMVHDYEKPLKGKVVGIPEEFWGEGMDPQVRESLEKSRELLVKAGMVLK
PVRLPSTQYAVNVYYLIATSEAASNLSRFDGIRYGERKTGARDLKELYEKSRGEGFGPEV
KRRILLGTFALSAGYQDQYYRKAQKVQALIREEFMRSFSECDLLFAPVTPTPAFRFGEKI
SDPLSMYLSDIFTISANLAGLPALSTPSFPTSNGLPVGAQLIGPHWSEGVLLKAASVLHE
GVHPGLAPWKGGS
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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