SitesBLAST
Comparing WP_043743836.1 NCBI__GCF_000009985.1:WP_043743836.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
52% identity, 96% coverage: 16:483/490 of query aligns to 25:478/485 of 2f2aA
- active site: K79 (= K78), S154 (= S159), S155 (= S160), S173 (≠ T178), T175 (= T180), G176 (= G181), G177 (= G182), S178 (= S183), Q181 (= Q186)
- binding glutamine: G130 (= G129), S154 (= S159), D174 (= D179), T175 (= T180), G176 (= G181), S178 (= S183), F206 (= F211), Y309 (= Y314), Y310 (= Y315), R358 (= R362), D425 (= D429)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
52% identity, 96% coverage: 16:483/490 of query aligns to 25:478/485 of 2dqnA
- active site: K79 (= K78), S154 (= S159), S155 (= S160), S173 (≠ T178), T175 (= T180), G176 (= G181), G177 (= G182), S178 (= S183), Q181 (= Q186)
- binding asparagine: M129 (= M128), G130 (= G129), T175 (= T180), G176 (= G181), S178 (= S183), Y309 (= Y314), Y310 (= Y315), R358 (= R362), D425 (= D429)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
48% identity, 96% coverage: 8:478/490 of query aligns to 6:466/478 of 3h0mA
- active site: K72 (= K78), S147 (= S159), S148 (= S160), S166 (≠ T178), T168 (= T180), G169 (= G181), G170 (= G182), S171 (= S183), Q174 (= Q186)
- binding glutamine: M122 (= M128), G123 (= G129), D167 (= D179), T168 (= T180), G169 (= G181), G170 (= G182), S171 (= S183), F199 (= F211), Y302 (= Y314), R351 (= R362), D418 (= D429)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
48% identity, 96% coverage: 8:478/490 of query aligns to 6:466/478 of 3h0lA
- active site: K72 (= K78), S147 (= S159), S148 (= S160), S166 (≠ T178), T168 (= T180), G169 (= G181), G170 (= G182), S171 (= S183), Q174 (= Q186)
- binding asparagine: G123 (= G129), S147 (= S159), G169 (= G181), G170 (= G182), S171 (= S183), Y302 (= Y314), R351 (= R362), D418 (= D429)
3kfuE Crystal structure of the transamidosome (see paper)
46% identity, 96% coverage: 11:480/490 of query aligns to 4:456/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
37% identity, 82% coverage: 69:471/490 of query aligns to 29:443/450 of 4n0iA
- active site: K38 (= K78), S116 (= S159), S117 (= S160), T135 (= T178), T137 (= T180), G138 (= G181), G139 (= G182), S140 (= S183), L143 (≠ Q186)
- binding glutamine: G89 (= G129), T137 (= T180), G138 (= G181), S140 (= S183), Y168 (≠ F211), Y271 (= Y314), Y272 (= Y315), R320 (= R362), D404 (= D429)
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
31% identity, 89% coverage: 51:487/490 of query aligns to 177:597/607 of Q7XJJ7
- K205 (= K78) 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)
31% identity, 89% coverage: 51:487/490 of query aligns to 177:597/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A127), T258 (≠ S130), S281 (= S159), G302 (≠ T180), G303 (= G181), S305 (= S183), S472 (≠ T367), I532 (≠ D421), M539 (≠ N428)
Sites not aligning to the query:
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
34% identity, 84% coverage: 68:478/490 of query aligns to 85:497/508 of 3a1iA
- active site: K95 (= K78), S170 (= S159), S171 (= S160), G189 (≠ T178), Q191 (≠ T180), G192 (= G181), G193 (= G182), A194 (≠ S183), I197 (≠ Q186)
- binding benzamide: F145 (≠ M128), S146 (≠ G129), G147 (≠ S130), Q191 (≠ T180), G192 (= G181), G193 (= G182), A194 (≠ S183), W327 (≠ Y314)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
31% identity, 96% coverage: 7:478/490 of query aligns to 1:448/457 of 6c6gA
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
31% identity, 97% coverage: 5:478/490 of query aligns to 6:476/487 of 1m21A
- active site: K81 (= K78), S160 (= S159), S161 (= S160), T179 (= T178), T181 (= T180), D182 (≠ G181), G183 (= G182), S184 (= S183), C187 (≠ Q186)
- binding : A129 (= A127), N130 (≠ M128), F131 (≠ G129), C158 (≠ G157), G159 (= G158), S160 (= S159), S184 (= S183), C187 (≠ Q186), I212 (≠ F211), R318 (≠ Y315), L321 (≠ A318), L365 (= L364), F426 (≠ D421)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
29% identity, 97% coverage: 3:479/490 of query aligns to 24:488/507 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 (= 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 (≠ D376) 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 (≠ D429) 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.
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
26% identity, 95% coverage: 5:471/490 of query aligns to 3:437/457 of 5h6sC
- active site: K77 (= K78), S152 (= S159), S153 (= S160), L173 (≠ T180), G174 (= G181), G175 (= G182), S176 (= S183)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A127), R128 (≠ G129), W129 (≠ S130), S152 (= S159), L173 (≠ T180), G174 (= G181), S176 (= S183), W306 (≠ Y314), F338 (≠ I365)
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
26% identity, 97% coverage: 3:479/490 of query aligns to 1:550/564 of 6te4A
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
28% identity, 95% coverage: 3:467/490 of query aligns to 18:450/605 of Q936X2
- K91 (= K78) mutation to A: Loss of activity.
- S165 (≠ K153) mutation to A: Loss of activity.
- S189 (= S183) 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)
27% identity, 89% coverage: 25:462/490 of query aligns to 24:457/490 of 4yjiA
- active site: K79 (= K78), S158 (= S159), S159 (= S160), G179 (≠ T180), G180 (= G181), G181 (= G182), A182 (≠ S183)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L80), G132 (≠ A127), S158 (= S159), G179 (≠ T180), G180 (= G181), A182 (≠ S183)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
30% identity, 94% coverage: 16:474/490 of query aligns to 12:434/461 of 4gysB
- active site: K72 (= K78), S146 (= S159), S147 (= S160), T165 (= T178), T167 (= T180), A168 (≠ G181), G169 (= G182), S170 (= S183), V173 (≠ Q186)
- binding malonate ion: A120 (= A127), G122 (= G129), S146 (= S159), T167 (= T180), A168 (≠ G181), S170 (= S183), S193 (≠ F206), G194 (= G207), V195 (≠ I208), R200 (≠ S213), Y297 (= Y329), 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)
39% identity, 31% coverage: 70:223/490 of query aligns to 28:177/425 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 (= 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.
Sites not aligning to the query:
- 214 S→T: Slightly reduces catalytic activity.
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
27% identity, 93% coverage: 24:480/490 of query aligns to 11:409/412 of 1o9oA
- active site: K62 (= K78), A131 (≠ S159), S132 (= S160), T150 (= T178), T152 (= T180), G153 (= G181), G154 (= G182), S155 (= S183), R158 (≠ Q186)
- binding 3-amino-3-oxopropanoic acid: G130 (≠ A152), T152 (= T180), G153 (= G181), G154 (= G182), S155 (= S183), R158 (≠ Q186), P359 (= P422)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
27% identity, 93% coverage: 24:480/490 of query aligns to 11:409/412 of 1ocmA
- active site: K62 (= K78), S131 (vs. gap), S132 (= S160), T152 (= T180), G153 (= G181), G154 (= G182), S155 (= S183)
- binding pyrophosphate 2-: R113 (≠ S148), S131 (vs. gap), Q151 (≠ D179), T152 (= T180), G153 (= G181), G154 (= G182), S155 (= S183), R158 (≠ Q186), P359 (= P422)
Query Sequence
>WP_043743836.1 NCBI__GCF_000009985.1:WP_043743836.1
MSKLTDLTMAEARDGLAKGAFTAVELTDAHIKATEAQRHLNAFIVETPDLALEAAKASDA
RRQAGTAGSMDGLPIGIKDLFCTEGVQTTAASHILEGFKPPYESTVSGKLKAAGAISLGK
LNLDEFAMGSSNQTSYFGAVENPWKKTSDPKAKLVPGGSSGGSAAAVAARMVLGATGTDT
GGSIRQPAAFCGITGIKPTYGRCSRFGIVAFASSLDQAGPMARTVRDCAIMLGAMAGHDP
KDSTSVNMAVPDFERALTGDIRGLKVGIPKEYRPDGLSDEVAKVWDRGIEWLKAAGATPV
EISLPHTKYALATYYIIAPAECSSNLARYDGLRYGLRVPGKTLDDMYKKSRAAGFGAEVR
RRILIGTYVLSAGYYDAYYAKAQKVRRLIAEDFRKAFETVDVILTPTAPSAAFGMGEGTD
DPVTMWLNDVFTIPTSMAGLPGLSLPAGLSADGLPLGLQLIGRPFDEETVFRVAGVMETA
ANFTAKPEGV
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