SitesBLAST
Comparing WP_012566706.1 NCBI__GCF_000016185.1:WP_012566706.1 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)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
46% identity, 97% coverage: 2:508/521 of query aligns to 1:473/485 of 2f2aA
- active site: K79 (= K78), S154 (= S189), S155 (= S190), S173 (≠ T208), T175 (= T210), G176 (= G211), G177 (= G212), S178 (= S213), Q181 (= Q216)
- binding glutamine: G130 (= G129), S154 (= S189), D174 (= D209), T175 (= T210), G176 (= G211), S178 (= S213), F206 (= F241), Y309 (= Y344), Y310 (= Y345), R358 (= R392), D425 (= D459)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
46% identity, 97% coverage: 2:508/521 of query aligns to 1:473/485 of 2dqnA
- active site: K79 (= K78), S154 (= S189), S155 (= S190), S173 (≠ T208), T175 (= T210), G176 (= G211), G177 (= G212), S178 (= S213), Q181 (= Q216)
- binding asparagine: M129 (= M128), G130 (= G129), T175 (= T210), G176 (= G211), S178 (= S213), Y309 (= Y344), Y310 (= Y345), R358 (= R392), D425 (= D459)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
47% identity, 96% coverage: 8:509/521 of query aligns to 6:467/478 of 3h0mA
- active site: K72 (= K78), S147 (= S189), S148 (= S190), S166 (≠ T208), T168 (= T210), G169 (= G211), G170 (= G212), S171 (= S213), Q174 (= Q216)
- binding glutamine: M122 (= M128), G123 (= G129), D167 (= D209), T168 (= T210), G169 (= G211), G170 (= G212), S171 (= S213), F199 (= F241), Y302 (= Y344), R351 (= R392), D418 (= D459)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
47% identity, 96% coverage: 8:509/521 of query aligns to 6:467/478 of 3h0lA
- active site: K72 (= K78), S147 (= S189), S148 (= S190), S166 (≠ T208), T168 (= T210), G169 (= G211), G170 (= G212), S171 (= S213), Q174 (= Q216)
- binding asparagine: G123 (= G129), S147 (= S189), G169 (= G211), G170 (= G212), S171 (= S213), Y302 (= Y344), R351 (= R392), D418 (= D459)
3kfuE Crystal structure of the transamidosome (see paper)
44% identity, 94% coverage: 19:510/521 of query aligns to 12:456/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
35% identity, 83% coverage: 70:501/521 of query aligns to 30:443/450 of 4n0iA
- active site: K38 (= K78), S116 (= S189), S117 (= S190), T135 (= T208), T137 (= T210), G138 (= G211), G139 (= G212), S140 (= S213), L143 (≠ Q216)
- binding glutamine: G89 (= G129), T137 (= T210), G138 (= G211), S140 (= S213), Y168 (≠ F241), Y271 (= Y344), Y272 (= Y345), R320 (= R392), D404 (= D459)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
29% identity, 86% coverage: 70:517/521 of query aligns to 87:506/508 of 3a1iA
- active site: K95 (= K78), S170 (≠ E177), S171 (≠ W178), G189 (≠ T208), Q191 (≠ T210), G192 (= G211), G193 (= G212), A194 (≠ S213), I197 (≠ Q216)
- binding benzamide: F145 (≠ M128), S146 (≠ G129), G147 (≠ S130), Q191 (≠ T210), G192 (= G211), G193 (= G212), A194 (≠ S213), W327 (≠ Y344)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
33% identity, 96% coverage: 9:509/521 of query aligns to 8:477/487 of 1m21A
- active site: K81 (= K78), S160 (= S189), S161 (= S190), T179 (= T208), T181 (= T210), D182 (≠ G211), G183 (= G212), S184 (= S213), C187 (≠ Q216)
- binding : A129 (= A127), N130 (≠ M128), F131 (≠ G129), C158 (≠ G187), G159 (= G188), S160 (= S189), S184 (= S213), C187 (≠ Q216), I212 (≠ F241), R318 (≠ Y345), L321 (≠ A348), L365 (= L394), F426 (≠ Y456)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
30% identity, 98% coverage: 7:517/521 of query aligns to 28:496/507 of Q84DC4
- T31 (≠ A10) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K78) mutation to A: Abolishes activity on mandelamide.
- S180 (= S189) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S190) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G211) 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 (= S213) mutation to A: Abolishes activity on mandelamide.
- Q207 (= Q216) 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 (≠ A325) 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 (≠ D406) 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 (vs. gap) 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.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
28% identity, 89% coverage: 48:511/521 of query aligns to 174:591/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A127), T258 (≠ S130), S281 (= S189), G302 (≠ T210), G303 (= G211), S305 (= S213), S472 (≠ T397), I532 (≠ A454), M539 (vs. gap)
Sites not aligning to the query:
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, 89% coverage: 48:511/521 of query aligns to 174:591/607 of Q7XJJ7
- K205 (= K78) mutation to A: Loss of activity.
- SS 281:282 (= SS 189:190) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 210:213) binding substrate
- S305 (= S213) mutation to A: Loss of activity.
- R307 (= R215) mutation to A: Loss of activity.
- S360 (≠ F268) mutation to A: No effect.
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
28% identity, 97% coverage: 7:509/521 of query aligns to 1:449/457 of 6c6gA
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
28% identity, 89% coverage: 48:511/521 of query aligns to 174:591/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A127), G302 (≠ T210), G303 (= G211), G304 (= G212), A305 (≠ S213), V442 (≠ Y345), I475 (≠ L400), M539 (vs. gap)
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, 89% coverage: 48:511/521 of query aligns to 174:591/605 of 8ey1D
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
27% identity, 97% coverage: 7:511/521 of query aligns to 5:447/457 of 5h6sC
- active site: K77 (= K78), S152 (= S189), S153 (= S190), L173 (≠ T210), G174 (= G211), G175 (= G212), S176 (= S213)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A127), R128 (≠ G129), W129 (≠ S130), S152 (= S189), L173 (≠ T210), G174 (= G211), S176 (= S213), W306 (≠ Y344), F338 (≠ I395)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
30% identity, 89% coverage: 52:513/521 of query aligns to 48:443/461 of 4gysB
- active site: K72 (= K78), S146 (= S189), S147 (= S190), T165 (= T208), T167 (= T210), A168 (≠ G211), G169 (= G212), S170 (= S213), V173 (≠ Q216)
- binding malonate ion: A120 (= A127), G122 (= G129), S146 (= S189), T167 (= T210), A168 (≠ G211), S170 (= S213), S193 (≠ W236), G194 (= G237), V195 (≠ I238), R200 (≠ S243), Y297 (= Y359), R305 (= R367)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
30% identity, 86% coverage: 51:500/521 of query aligns to 64:453/605 of Q936X2
- K91 (= K78) mutation to A: Loss of activity.
- S165 (= S189) mutation to A: Loss of activity.
- S189 (= S213) mutation to A: Loss of activity.
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
24% identity, 96% coverage: 10:511/521 of query aligns to 9:476/490 of 4yjiA
- active site: K79 (= K78), S158 (≠ A157), S159 (≠ G158), G179 (≠ T210), G180 (= G211), G181 (= G212), A182 (≠ S213)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L80), G132 (≠ A127), S158 (≠ A157), G179 (≠ T210), G180 (= G211), A182 (≠ S213)
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, 39% coverage: 70:270/521 of query aligns to 28:197/425 of Q9FR37
- K36 (= K78) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S189) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S190) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D209) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S213) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (≠ V221) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 214 S→T: Slightly reduces catalytic activity.
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
27% identity, 54% coverage: 16:298/521 of query aligns to 14:259/482 of 3a2qA
- active site: K69 (= K78), S147 (≠ D153), S148 (≠ A154), N166 (≠ T208), A168 (≠ T210), A169 (≠ G211), G170 (= G212), A171 (≠ S213), I174 (≠ Q216)
- binding 6-aminohexanoic acid: G121 (≠ A127), G121 (≠ A127), N122 (≠ M128), S147 (≠ D153), A168 (≠ T210), A168 (≠ T210), A169 (≠ G211), A171 (≠ S213)
Sites not aligning to the query:
Query Sequence
>WP_012566706.1 NCBI__GCF_000016185.1:WP_012566706.1
MMSLNHLTMAEALAGLRAGEFTATELTEAHLRAVEATRGLNIFITETADIALRQAKAADE
RYAAGTALPMDGLPIAVKDLFCTEGVLTTAASHILDGFKPPYESSVTANLWRDGAVMLGK
VNLDEFAMGSANITSYYGPVISPWSKGRRVQRDAAPAGSGVLSEVAEAFRQPQPVTEWEW
ERRLVPGGSSGGSAAAVAARVAMAATGTDTGGSIRQPASFVGIVGLKPTYGRCSRWGIVA
FASSLDQAGPMTRTVRDAAIMLRSMAGFDPKDSTSADVPVPDYEKAITGDIRGLRVGIPR
EYRVDGMPAEIDRLWQQGVEWLKAAGAVPVEISLPHTKYALPAYYIVAPAEASSNLARYD
GVRFGLRVEGKDLKEMYENTRGEGFGREVRRRILIGTYVLSAGYYDAYYLKAQKVRARIA
EDFTKAWEQCDVILTPTAPNTAFGIGEKMDDPIAMYLNDVFTVPANLAGLPGLSVPAGLA
ANGLPLGLQLVGRPFDEATLIRTAAVLEQAAGPQPLPPVHA
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