SitesBLAST
Comparing WP_007475355.1 NCBI__GCF_000170735.1:WP_007475355.1 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)
56% identity, 88% coverage: 50:448/451 of query aligns to 66:470/478 of 3h0mA
- active site: K72 (= K56), S147 (= S131), S148 (= S132), S166 (= S150), T168 (= T152), G169 (= G153), G170 (= G154), S171 (= S155), Q174 (= Q158)
- binding glutamine: M122 (= M106), G123 (= G107), D167 (= D151), T168 (= T152), G169 (= G153), G170 (= G154), S171 (= S155), F199 (= F183), Y302 (= Y282), R351 (= R329), D418 (= D395)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
56% identity, 88% coverage: 50:448/451 of query aligns to 66:470/478 of 3h0lA
- active site: K72 (= K56), S147 (= S131), S148 (= S132), S166 (= S150), T168 (= T152), G169 (= G153), G170 (= G154), S171 (= S155), Q174 (= Q158)
- binding asparagine: G123 (= G107), S147 (= S131), G169 (= G153), G170 (= G154), S171 (= S155), Y302 (= Y282), R351 (= R329), D418 (= D395)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
55% identity, 87% coverage: 50:440/451 of query aligns to 73:469/485 of 2f2aA
- active site: K79 (= K56), S154 (= S131), S155 (= S132), S173 (= S150), T175 (= T152), G176 (= G153), G177 (= G154), S178 (= S155), Q181 (= Q158)
- binding glutamine: G130 (= G107), S154 (= S131), D174 (= D151), T175 (= T152), G176 (= G153), S178 (= S155), F206 (= F183), Y309 (= Y282), Y310 (= Y283), R358 (= R329), D425 (= D395)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
55% identity, 87% coverage: 50:440/451 of query aligns to 73:469/485 of 2dqnA
- active site: K79 (= K56), S154 (= S131), S155 (= S132), S173 (= S150), T175 (= T152), G176 (= G153), G177 (= G154), S178 (= S155), Q181 (= Q158)
- binding asparagine: M129 (= M106), G130 (= G107), T175 (= T152), G176 (= G153), S178 (= S155), Y309 (= Y282), Y310 (= Y283), R358 (= R329), D425 (= D395)
3kfuE Crystal structure of the transamidosome (see paper)
44% identity, 95% coverage: 17:445/451 of query aligns to 18:455/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
35% identity, 88% coverage: 50:446/451 of query aligns to 32:449/450 of 4n0iA
- active site: K38 (= K56), S116 (= S131), S117 (= S132), T135 (≠ S150), T137 (= T152), G138 (= G153), G139 (= G154), S140 (= S155), L143 (≠ Q158)
- binding glutamine: G89 (= G107), T137 (= T152), G138 (= G153), S140 (= S155), Y168 (≠ F183), Y271 (= Y282), Y272 (= Y283), R320 (= R329), D404 (= D395)
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
29% identity, 89% coverage: 49:451/451 of query aligns to 198:595/607 of Q7XJJ7
- K205 (= K56) mutation to A: Loss of activity.
- SS 281:282 (= SS 131:132) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 152:155) binding substrate
- S305 (= S155) mutation to A: Loss of activity.
- R307 (= R157) mutation to A: Loss of activity.
- S360 (≠ Y210) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
29% identity, 89% coverage: 49:451/451 of query aligns to 198:595/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A105), T258 (≠ S108), S281 (= S131), G302 (≠ T152), G303 (= G153), S305 (= S155), S472 (≠ Q321), I532 (≠ D387), M539 (≠ S394)
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
29% identity, 89% coverage: 49:451/451 of query aligns to 198:595/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A105), G302 (≠ T152), G303 (= G153), G304 (= G154), A305 (≠ S155), V442 (= V284), I475 (≠ M331), M539 (≠ S394)
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
29% identity, 89% coverage: 49:451/451 of query aligns to 198:595/605 of 8ey1D
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
30% identity, 88% coverage: 50:445/451 of query aligns to 68:449/457 of 6c6gA
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
29% identity, 90% coverage: 39:446/451 of query aligns to 74:499/508 of 3a1iA
- active site: K95 (= K56), S170 (= S131), S171 (= S132), G189 (≠ S150), Q191 (≠ T152), G192 (= G153), G193 (= G154), A194 (≠ S155), I197 (≠ Q158)
- binding benzamide: F145 (≠ M106), S146 (≠ G107), G147 (≠ S108), Q191 (≠ T152), G192 (= G153), G193 (= G154), A194 (≠ S155), W327 (≠ Y282)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
29% identity, 88% coverage: 50:447/451 of query aligns to 94:490/507 of Q84DC4
- K100 (= K56) mutation to A: Abolishes activity on mandelamide.
- S180 (= S131) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S132) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G153) 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 (= S155) mutation to A: Abolishes activity on mandelamide.
- Q207 (= Q158) 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 (≠ D278) 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 (≠ D343) 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 (= I396) 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.
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
29% identity, 89% coverage: 50:451/451 of query aligns to 75:483/487 of 1m21A
- active site: K81 (= K56), S160 (= S131), S161 (= S132), T179 (≠ S150), T181 (= T152), D182 (≠ G153), G183 (= G154), S184 (= S155), C187 (≠ Q158)
- binding : A129 (= A105), N130 (vs. gap), F131 (vs. gap), C158 (≠ G129), G159 (= G130), S160 (= S131), S184 (= S155), C187 (≠ Q158), I212 (≠ F183), R318 (≠ S292), L321 (≠ A295), L365 (≠ V336), F426 (vs. gap)
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)
25% identity, 85% coverage: 49:430/451 of query aligns to 29:408/425 of Q9FR37
- K36 (= K56) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S131) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S132) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D151) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S155) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C163) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (≠ D246) mutation to T: Slightly reduces catalytic activity.
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
29% identity, 88% coverage: 50:444/451 of query aligns to 63:468/482 of 3a2qA
- active site: K69 (= K56), S147 (= S131), S148 (= S132), N166 (≠ S150), A168 (≠ T152), A169 (≠ G153), G170 (= G154), A171 (≠ S155), I174 (≠ Q158)
- binding 6-aminohexanoic acid: G121 (≠ A105), G121 (≠ A105), N122 (≠ M106), S147 (= S131), A168 (≠ T152), A168 (≠ T152), A169 (≠ G153), A171 (≠ S155), C313 (≠ A286)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
29% identity, 86% coverage: 50:436/451 of query aligns to 66:430/461 of 4gysB
- active site: K72 (= K56), S146 (= S131), S147 (= S132), T165 (≠ S150), T167 (= T152), A168 (≠ G153), G169 (= G154), S170 (= S155), V173 (≠ Q158)
- binding malonate ion: A120 (= A105), G122 (= G107), S146 (= S131), T167 (= T152), A168 (≠ G153), S170 (= S155), S193 (≠ Y178), G194 (= G179), V195 (≠ L180), R200 (≠ S185), Y297 (≠ F297), R305 (= R305)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
28% identity, 86% coverage: 50:436/451 of query aligns to 85:453/605 of Q936X2
- K91 (= K56) mutation to A: Loss of activity.
- S165 (= S131) mutation to A: Loss of activity.
- S189 (= S155) mutation to A: Loss of activity.
Q9MUK5 Translocon at the outer membrane of chloroplasts 64 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
23% identity, 80% coverage: 88:449/451 of query aligns to 103:456/593 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.
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)
31% identity, 49% coverage: 50:268/451 of query aligns to 136:361/579 of Q9TUI8
- S217 (= S131) mutation to A: Loss of activity.
- S218 (= S132) mutation to A: Lowers activity by at least 98%.
- D237 (= D151) mutation D->E,N: Loss of activity.
- S241 (= S155) mutation to A: Loss of activity.
- C249 (= C163) mutation to A: Loss of activity.
Query Sequence
>WP_007475355.1 NCBI__GCF_000170735.1:WP_007475355.1
MITLKDALNLPKEEIKELKKDINKKAKEEKSLGGYIEQFLDSDLAESGDGVPIAIKDNIN
VKGWEITCASKILKGYKAPYNATVIDKMFENGLSAYGRCNMDEFAMGSSTETSQYGKTLN
PHNPNRVPGGSSGGSAAVVGANLAIAALGSDTGGSIRQPAAFCGVVGMKPTYGRVSRYGL
VAFSSSLDQIGPITQNVEDAAILYNIIAGYDKNDSTSARIDHTPVEINENRKLKIAVIDN
YIDEADNEIKNAILDVIKGLEKEGHTIIHKNLMNSKIDVATYYVVATAEASSNLARFDGM
RYGNRIEGKDLKETYKLTRAQFGDEVKRRIMLGTFVLSSGYYDAYYIKAQKVRHIIKNEF
DKLFAEADVIITPVTPTTAFEFGSKKDPLEMYLSDIYTISVNLAGVPAISLPIAKDKESM
PIGMQIIAKHFDEQSLFDAAKIVENIVKDSK
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