SitesBLAST
Comparing WP_012050569.1 NCBI__GCF_000016765.1:WP_012050569.1 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)
35% identity, 95% coverage: 11:437/450 of query aligns to 4:455/468 of 3kfuE
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
28% identity, 96% coverage: 9:442/450 of query aligns to 8:479/485 of 2f2aA
- active site: K79 (= K80), S154 (= S153), S155 (= S154), S173 (≠ T172), T175 (= T174), G176 (= G175), G177 (= G176), S178 (= S177), Q181 (≠ L180)
- binding glutamine: G130 (≠ V131), S154 (= S153), D174 (= D173), T175 (= T174), G176 (= G175), S178 (= S177), F206 (≠ S205), Y309 (≠ A288), Y310 (≠ E289), R358 (≠ T324), D425 (vs. gap)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
28% identity, 96% coverage: 9:442/450 of query aligns to 8:479/485 of 2dqnA
- active site: K79 (= K80), S154 (= S153), S155 (= S154), S173 (≠ T172), T175 (= T174), G176 (= G175), G177 (= G176), S178 (= S177), Q181 (≠ L180)
- binding asparagine: M129 (≠ F130), G130 (≠ V131), T175 (= T174), G176 (= G175), S178 (= S177), Y309 (≠ A288), Y310 (≠ E289), R358 (≠ T324), D425 (vs. gap)
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, 94% coverage: 16:439/450 of query aligns to 138:591/607 of Q7XJJ7
- K205 (= K80) mutation to A: Loss of activity.
- SS 281:282 (= SS 153:154) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 174:177) binding substrate
- S305 (= S177) mutation to A: Loss of activity.
- R307 (= R179) mutation to A: Loss of activity.
- S360 (≠ G232) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
28% identity, 94% coverage: 16:439/450 of query aligns to 138:591/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (vs. gap), T258 (= T126), S281 (= S153), G302 (≠ T174), G303 (= G175), S305 (= S177), S472 (≠ A322), I532 (≠ M379), M539 (≠ A387)
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
28% identity, 94% coverage: 16:439/450 of query aligns to 138:591/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (vs. gap), G302 (≠ T174), G303 (= G175), G304 (= G176), A305 (≠ S177), V442 (≠ G295), I475 (= I325), M539 (≠ A387)
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
28% identity, 94% coverage: 16:439/450 of query aligns to 138:591/605 of 8ey1D
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 97% coverage: 9:446/450 of query aligns to 7:476/478 of 3h0mA
- active site: K72 (= K80), S147 (= S153), S148 (= S154), S166 (≠ T172), T168 (= T174), G169 (= G175), G170 (= G176), S171 (= S177), Q174 (≠ L180)
- binding glutamine: M122 (≠ A127), G123 (= G128), D167 (= D173), T168 (= T174), G169 (= G175), G170 (= G176), S171 (= S177), F199 (≠ S205), Y302 (≠ A288), R351 (≠ T324), D418 (≠ A387)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 97% coverage: 9:446/450 of query aligns to 7:476/478 of 3h0lA
- active site: K72 (= K80), S147 (= S153), S148 (= S154), S166 (≠ T172), T168 (= T174), G169 (= G175), G170 (= G176), S171 (= S177), Q174 (≠ L180)
- binding asparagine: G123 (= G128), S147 (= S153), G169 (= G175), G170 (= G176), S171 (= S177), Y302 (≠ A288), R351 (≠ T324), D418 (≠ A387)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
31% identity, 87% coverage: 40:429/450 of query aligns to 15:400/412 of 1o9oA
- active site: K62 (= K80), A131 (≠ S153), S132 (= S154), T150 (= T172), T152 (= T174), G153 (= G175), G154 (= G176), S155 (= S177), R158 (≠ L180)
- binding 3-amino-3-oxopropanoic acid: G130 (≠ M152), T152 (= T174), G153 (= G175), G154 (= G176), S155 (= S177), R158 (≠ L180), P359 (= P384)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
31% identity, 90% coverage: 32:436/450 of query aligns to 26:448/457 of 6c6gA
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
31% identity, 87% coverage: 40:429/450 of query aligns to 15:400/412 of 1ocmA
- active site: K62 (= K80), S131 (= S153), S132 (= S154), T152 (= T174), G153 (= G175), G154 (= G176), S155 (= S177)
- binding pyrophosphate 2-: R113 (≠ V131), S131 (= S153), Q151 (≠ D173), T152 (= T174), G153 (= G175), G154 (= G176), S155 (= S177), R158 (≠ L180), P359 (= P384)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
31% identity, 82% coverage: 70:438/450 of query aligns to 85:499/508 of 3a1iA
- active site: K95 (= K80), S170 (= S153), S171 (= S154), G189 (≠ T172), Q191 (≠ T174), G192 (= G175), G193 (= G176), A194 (≠ S177), I197 (≠ L180)
- binding benzamide: F145 (vs. gap), S146 (≠ A127), G147 (= G128), Q191 (≠ T174), G192 (= G175), G193 (= G176), A194 (≠ S177), W327 (= W300)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
30% identity, 96% coverage: 6:437/450 of query aligns to 5:477/487 of 1m21A
- active site: K81 (= K80), S160 (= S153), S161 (= S154), T179 (= T172), T181 (= T174), D182 (≠ G175), G183 (= G176), S184 (= S177), C187 (≠ L180)
- binding : A129 (= A129), N130 (vs. gap), F131 (vs. gap), C158 (≠ G151), G159 (≠ M152), S160 (= S153), S184 (= S177), C187 (≠ L180), I212 (≠ S205), R318 (≠ G295), L321 (≠ Q298), L365 (vs. gap), F426 (≠ L385)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
30% identity, 97% coverage: 2:438/450 of query aligns to 23:489/507 of Q84DC4
- T31 (= T10) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K80) mutation to A: Abolishes activity on mandelamide.
- S180 (= S153) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S154) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G175) 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 (= S177) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ L180) 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 (≠ L291) 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 (≠ D338) 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 (≠ A387) 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.
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)
27% identity, 72% coverage: 106:429/450 of query aligns to 64:415/425 of Q9FR37
- S113 (= S153) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S154) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D173) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S177) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C185) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (≠ A244) mutation to T: Slightly reduces catalytic activity.
Sites not aligning to the query:
- 36 active site, Charge relay system; K→A: Loss of catalytic activity.; K→R: Reduces catalytic activity 10-fold.
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
28% identity, 96% coverage: 11:443/450 of query aligns to 10:480/490 of 4yjiA
- active site: K79 (= K80), S158 (= S153), S159 (= S154), G179 (≠ T174), G180 (= G175), G181 (= G176), A182 (≠ S177)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L82), G132 (≠ A129), S158 (= S153), G179 (≠ T174), G180 (= G175), A182 (≠ S177)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
32% identity, 82% coverage: 50:419/450 of query aligns to 45:421/461 of 4gysB
- active site: K72 (= K80), S146 (= S153), S147 (= S154), T165 (= T172), T167 (= T174), A168 (≠ G175), G169 (= G176), S170 (= S177), V173 (≠ L180)
- binding malonate ion: A120 (= A129), G122 (≠ V131), S146 (= S153), T167 (= T174), A168 (≠ G175), S170 (= S177), S193 (≠ E200), G194 (= G201), V195 (= V202), R200 (≠ P207), Y297 (≠ L291), R305 (≠ A299)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
27% identity, 97% coverage: 3:437/450 of query aligns to 1:445/457 of 5h6sC
- active site: K77 (= K80), S152 (= S153), S153 (= S154), L173 (≠ T174), G174 (= G175), G175 (= G176), S176 (= S177)
- binding 4-oxidanylbenzohydrazide: C126 (vs. gap), R128 (≠ K122), W129 (≠ T123), S152 (= S153), L173 (≠ T174), G174 (= G175), S176 (= S177), W306 (≠ F272), F338 (≠ A303)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
29% identity, 82% coverage: 68:435/450 of query aligns to 76:460/605 of Q936X2
- K91 (= K80) mutation to A: Loss of activity.
- S165 (= S153) mutation to A: Loss of activity.
- S189 (= S177) mutation to A: Loss of activity.
Query Sequence
>WP_012050569.1 NCBI__GCF_000016765.1:WP_012050569.1
MDEAFDLDVTELGSRYRDRTLSPVEVEQGLSARIARLDPELGAFTALAGEEARTAARQAE
AELAAGIDRGPLHGVPVTVKDLCLTRDMPTAAGLRGFAERLPRRDAAVVARLREAGAVLV
GKTYTTAGAFVDPAADRPFPRHPGRADIFPGMSSTGAGVAVAAGLCSVAIGTDTGGSIRL
PSMCCGVSGFKPAYRRVDAEGVFESAPSLDHVGPIARSVADLAAAMTAIGEGESPRALVT
DLAAVRIGVDRRALELTGPKSRGAIERAIGLFGELGVTAVEVTLPPVAELLAATGRLQAW
ETAAVHAAWYPAHRGDYGPGLAATIDRGRAMQAGDLDDFEAVRAAYRQQLDALFATVDLI
ILPVLTIDTPTLDEWEGAMRQADPLGARFTKPFNVTGHPALALPGGFDADGLPLGFQLVA
RPADEAFLLGAGVAFQKISDWHRGLPRALP
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