SitesBLAST
Comparing WP_012504996.1 NCBI__GCF_000020625.1:WP_012504996.1 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)
53% identity, 97% coverage: 4:465/477 of query aligns to 5:459/478 of 3h0mA
- active site: K72 (= K76), S147 (= S151), S148 (= S152), S166 (= S170), T168 (= T172), G169 (= G173), G170 (= G174), S171 (= S175), Q174 (= Q178)
- binding glutamine: M122 (= M126), G123 (= G127), D167 (= D171), T168 (= T172), G169 (= G173), G170 (= G174), S171 (= S175), F199 (= F203), Y302 (= Y307), R351 (= R356), D418 (= D423)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
53% identity, 97% coverage: 4:465/477 of query aligns to 5:459/478 of 3h0lA
- active site: K72 (= K76), S147 (= S151), S148 (= S152), S166 (= S170), T168 (= T172), G169 (= G173), G170 (= G174), S171 (= S175), Q174 (= Q178)
- binding asparagine: G123 (= G127), S147 (= S151), G169 (= G173), G170 (= G174), S171 (= S175), Y302 (= Y307), R351 (= R356), D418 (= D423)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
47% identity, 98% coverage: 1:468/477 of query aligns to 3:469/485 of 2f2aA
- active site: K79 (= K76), S154 (= S151), S155 (= S152), S173 (= S170), T175 (= T172), G176 (= G173), G177 (= G174), S178 (= S175), Q181 (= Q178)
- binding glutamine: G130 (= G127), S154 (= S151), D174 (= D171), T175 (= T172), G176 (= G173), S178 (= S175), F206 (= F203), Y309 (= Y307), Y310 (= Y308), R358 (= R356), D425 (= D423)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
47% identity, 98% coverage: 1:468/477 of query aligns to 3:469/485 of 2dqnA
- active site: K79 (= K76), S154 (= S151), S155 (= S152), S173 (= S170), T175 (= T172), G176 (= G173), G177 (= G174), S178 (= S175), Q181 (= Q178)
- binding asparagine: M129 (= M126), G130 (= G127), T175 (= T172), G176 (= G173), S178 (= S175), Y309 (= Y307), Y310 (= Y308), R358 (= R356), D425 (= D423)
3kfuE Crystal structure of the transamidosome (see paper)
44% identity, 98% coverage: 7:474/477 of query aligns to 3:456/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
39% identity, 85% coverage: 68:471/477 of query aligns to 30:449/450 of 4n0iA
- active site: K38 (= K76), S116 (= S151), S117 (= S152), T135 (≠ S170), T137 (= T172), G138 (= G173), G139 (= G174), S140 (= S175), L143 (≠ Q178)
- binding glutamine: G89 (= G127), T137 (= T172), G138 (= G173), S140 (= S175), Y168 (≠ F203), Y271 (= Y307), Y272 (= Y308), R320 (= R356), D404 (= D423)
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, 91% coverage: 46:477/477 of query aligns to 175:593/607 of Q7XJJ7
- K205 (= K76) mutation to A: Loss of activity.
- SS 281:282 (= SS 151:152) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 172:175) binding substrate
- S305 (= S175) mutation to A: Loss of activity.
- R307 (= R177) mutation to A: Loss of activity.
- S360 (≠ N230) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
30% identity, 91% coverage: 46:477/477 of query aligns to 175:593/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A125), T258 (≠ S128), S281 (= S151), G302 (≠ T172), G303 (= G173), S305 (= S175), S472 (≠ T361), I532 (≠ P416), M539 (≠ D423)
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
30% identity, 91% coverage: 46:477/477 of query aligns to 175:593/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A125), G302 (≠ T172), G303 (= G173), G304 (= G174), A305 (≠ S175), V442 (≠ Y308), I475 (≠ L364), M539 (≠ D423)
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
30% identity, 91% coverage: 46:477/477 of query aligns to 175:593/605 of 8ey1D
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
34% identity, 98% coverage: 8:473/477 of query aligns to 10:477/487 of 1m21A
- active site: K81 (= K76), S160 (= S151), S161 (= S152), T179 (≠ S170), T181 (= T172), D182 (≠ G173), G183 (= G174), S184 (= S175), C187 (≠ Q178)
- binding : A129 (= A125), N130 (≠ M126), F131 (≠ G127), C158 (≠ G149), G159 (= G150), S160 (= S151), S184 (= S175), C187 (≠ Q178), I212 (≠ F203), R318 (≠ Y308), L321 (≠ T311), L365 (≠ M358), F426 (≠ D415)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
30% identity, 99% coverage: 4:475/477 of query aligns to 15:451/457 of 6c6gA
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
31% identity, 86% coverage: 66:473/477 of query aligns to 85:498/508 of 3a1iA
- active site: K95 (= K76), S170 (= S151), S171 (= S152), G189 (≠ S170), Q191 (≠ T172), G192 (= G173), G193 (= G174), A194 (≠ S175), I197 (≠ Q178)
- binding benzamide: F145 (≠ M126), S146 (≠ G127), G147 (≠ S128), Q191 (≠ T172), G192 (= G173), G193 (= G174), A194 (≠ S175), W327 (≠ Y307)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
31% identity, 95% coverage: 11:464/477 of query aligns to 9:430/461 of 4gysB
- active site: K72 (= K76), S146 (= S151), S147 (= S152), T165 (≠ S170), T167 (= T172), A168 (≠ G173), G169 (= G174), S170 (= S175), V173 (≠ Q178)
- binding malonate ion: A120 (= A125), G122 (= G127), S146 (= S151), T167 (= T172), A168 (≠ G173), S170 (= S175), S193 (≠ Y198), G194 (= G199), V195 (= V200), R200 (≠ S205), Y297 (= Y307), R305 (= R321)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
29% identity, 96% coverage: 16:473/477 of query aligns to 40:488/507 of Q84DC4
- K100 (= K76) mutation to A: Abolishes activity on mandelamide.
- S180 (= S151) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S152) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G173) 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 (= S175) mutation to A: Abolishes activity on mandelamide.
- Q207 (= Q178) 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 (≠ G367) 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 (≠ V427) 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.
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
30% identity, 94% coverage: 23:470/477 of query aligns to 38:459/605 of Q936X2
- K91 (= K76) mutation to A: Loss of activity.
- S165 (= S151) mutation to A: Loss of activity.
- S189 (= S175) mutation to A: Loss of activity.
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
26% identity, 97% coverage: 8:472/477 of query aligns to 9:444/457 of 5h6sC
- active site: K77 (= K76), S152 (= S151), S153 (= S152), L173 (≠ T172), G174 (= G173), G175 (= G174), S176 (= S175)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A125), R128 (≠ G127), W129 (≠ S128), S152 (= S151), L173 (≠ T172), G174 (= G173), S176 (= S175), W306 (≠ L319), F338 (≠ L359)
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)
26% identity, 83% coverage: 68:465/477 of query aligns to 28:415/425 of Q9FR37
- K36 (= K76) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S151) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S152) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D171) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S175) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C183) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (≠ G260) mutation to T: Slightly reduces catalytic activity.
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
27% identity, 96% coverage: 1:457/477 of query aligns to 3:458/490 of 4yjiA
- active site: K79 (= K76), S158 (= S151), S159 (= S152), G179 (≠ T172), G180 (= G173), G181 (= G174), A182 (≠ S175)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ N78), G132 (≠ A125), S158 (= S151), G179 (≠ T172), G180 (= G173), A182 (≠ S175)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
26% identity, 99% coverage: 5:474/477 of query aligns to 3:409/412 of 1o9oA
- active site: K62 (= K76), A131 (≠ S151), S132 (= S152), T150 (≠ S170), T152 (= T172), G153 (= G173), G154 (= G174), S155 (= S175), R158 (≠ Q178)
- binding 3-amino-3-oxopropanoic acid: G130 (= G150), T152 (= T172), G153 (= G173), G154 (= G174), S155 (= S175), R158 (≠ Q178), P359 (= P416)
Query Sequence
>WP_012504996.1 NCBI__GCF_000020625.1:WP_012504996.1
MQFSSYRDLREKLLAREMSCEAVVTAYLQRIEATRDRNIYISVFYDEALRQARSLDRKLD
AGETPGKLFGMPMAIKDNISIEGTGLTCASKILSNYTAVYDATVIRRLKEEDAVFLGKVN
MDEFAMGSSNENSSFGPVPNPYDSTKVPGGSSGGSAAAVAGDLALVALGSDTGGSVRQPA
GFCNVVGLKPTYGRISRYGVVAFGSSFDQIGILSKNADDAAAVLGVIAGNDGSDATSSHN
QVPDYAAEMEGVSLRGLKIGIPKEYFPESLNSDVASVIQERLDLLRSLGAEMIPITLPES
DYAIAAYYILTTAEASSNLARFDGARYGYRSEKSSDLTDMYVNSRTEGFGEEVKRRIMLG
TYVLSAGYYDTYYKKAQQVRRVFLNRYREALANVDVIAGPTSPFPPFGIGDKMDDPLEMY
LADVFTVPASIAGIPALSVPVGFDSSGLPVGMQLIGNFFEEGKLLGTARAVQNAGKV
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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