SitesBLAST
Comparing WP_013531785.1 NCBI__GCF_000185905.1:WP_013531785.1 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)
45% identity, 94% coverage: 16:505/521 of query aligns to 15:469/485 of 2f2aA
- active site: K79 (= K79), S154 (= S187), S155 (= S188), S173 (≠ T206), T175 (= T208), G176 (= G209), G177 (= G210), S178 (= S211), Q181 (= Q214)
- binding glutamine: G130 (= G130), S154 (= S187), D174 (= D207), T175 (= T208), G176 (= G209), S178 (= S211), F206 (= F239), Y309 (= Y342), Y310 (= Y343), R358 (= R390), D425 (= D460)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
45% identity, 94% coverage: 16:505/521 of query aligns to 15:469/485 of 2dqnA
- active site: K79 (= K79), S154 (= S187), S155 (= S188), S173 (≠ T206), T175 (= T208), G176 (= G209), G177 (= G210), S178 (= S211), Q181 (= Q214)
- binding asparagine: M129 (= M129), G130 (= G130), T175 (= T208), G176 (= G209), S178 (= S211), Y309 (= Y342), Y310 (= Y343), R358 (= R390), D425 (= D460)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
43% identity, 98% coverage: 4:516/521 of query aligns to 2:473/478 of 3h0mA
- active site: K72 (= K79), S147 (= S187), S148 (= S188), S166 (≠ T206), T168 (= T208), G169 (= G209), G170 (= G210), S171 (= S211), Q174 (= Q214)
- binding glutamine: M122 (= M129), G123 (= G130), D167 (= D207), T168 (= T208), G169 (= G209), G170 (= G210), S171 (= S211), F199 (= F239), Y302 (= Y342), R351 (= R390), D418 (= D460)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
43% identity, 98% coverage: 4:516/521 of query aligns to 2:473/478 of 3h0lA
- active site: K72 (= K79), S147 (= S187), S148 (= S188), S166 (≠ T206), T168 (= T208), G169 (= G209), G170 (= G210), S171 (= S211), Q174 (= Q214)
- binding asparagine: G123 (= G130), S147 (= S187), G169 (= G209), G170 (= G210), S171 (= S211), Y302 (= Y342), R351 (= R390), D418 (= D460)
3kfuE Crystal structure of the transamidosome (see paper)
41% identity, 96% coverage: 11:511/521 of query aligns to 4:456/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
33% identity, 83% coverage: 70:502/521 of query aligns to 29:443/450 of 4n0iA
- active site: K38 (= K79), S116 (≠ T158), S117 (≠ H159), T135 (= T206), T137 (= T208), G138 (= G209), G139 (= G210), S140 (= S211), L143 (≠ Q214)
- binding glutamine: G89 (= G130), T137 (= T208), G138 (= G209), S140 (= S211), Y168 (≠ F239), Y271 (= Y342), Y272 (= Y343), R320 (= R390), D404 (= D460)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
30% identity, 98% coverage: 9:520/521 of query aligns to 8:487/487 of 1m21A
- active site: K81 (= K79), S160 (= S187), S161 (= S188), T179 (= T206), T181 (= T208), D182 (≠ G209), G183 (= G210), S184 (= S211), C187 (≠ Q214)
- binding : A129 (= A128), N130 (≠ M129), F131 (≠ G130), C158 (≠ G185), G159 (= G186), S160 (= S187), S184 (= S211), C187 (≠ Q214), I212 (≠ F239), R318 (≠ Y343), L321 (≠ A346), L365 (≠ M392), F426 (≠ I461)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
28% identity, 94% coverage: 22:509/521 of query aligns to 16:448/457 of 6c6gA
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
28% identity, 98% coverage: 4:513/521 of query aligns to 25:491/507 of Q84DC4
- T31 (≠ S10) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K79) mutation to A: Abolishes activity on mandelamide.
- S180 (= S187) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S188) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G209) 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 (= S211) mutation to A: Abolishes activity on mandelamide.
- Q207 (= Q214) 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 (= S331) 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 (≠ D404) 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 (= I461) 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.
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
27% identity, 86% coverage: 69:515/521 of query aligns to 85:503/508 of 3a1iA
- active site: K95 (= K79), S170 (≠ R175), S171 (= S176), G189 (= G202), Q191 (≠ T208), G192 (= G209), G193 (= G210), A194 (≠ S211), I197 (≠ Q214)
- binding benzamide: F145 (≠ M129), S146 (≠ G130), G147 (≠ S131), Q191 (≠ T208), G192 (= G209), G193 (= G210), A194 (≠ S211), W327 (≠ Y342)
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
27% identity, 88% coverage: 56:512/521 of query aligns to 181:591/607 of Q7XJJ7
- K205 (= K79) mutation to A: Loss of activity.
- SS 281:282 (= SS 187:188) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 208:211) binding substrate
- S305 (= S211) mutation to A: Loss of activity.
- R307 (= R213) mutation to A: Loss of activity.
- S360 (≠ V266) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
27% identity, 88% coverage: 56:512/521 of query aligns to 181:591/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A128), T258 (≠ S131), S281 (= S187), G302 (≠ T208), G303 (= G209), S305 (= S211), S472 (≠ T395), I532 (≠ M456), M539 (vs. gap)
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
27% identity, 88% coverage: 56:512/521 of query aligns to 181:591/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A128), G302 (≠ T208), G303 (= G209), G304 (= G210), A305 (≠ S211), V442 (≠ Y343), I475 (≠ L398), 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
27% identity, 88% coverage: 56:512/521 of query aligns to 181:591/605 of 8ey1D
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
25% identity, 95% coverage: 16:512/521 of query aligns to 15:476/490 of 4yjiA
- active site: K79 (= K79), S158 (≠ G170), S159 (≠ T171), G179 (≠ T208), G180 (= G209), G181 (= G210), A182 (≠ S211)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L81), G132 (≠ A128), S158 (≠ G170), G179 (≠ T208), G180 (= G209), A182 (≠ S211)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
25% identity, 98% coverage: 5:512/521 of query aligns to 3:447/457 of 5h6sC
- active site: K77 (= K79), S152 (= S187), S153 (= S188), L173 (≠ T208), G174 (= G209), G175 (= G210), S176 (= S211)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A128), R128 (≠ G130), W129 (≠ S131), S152 (= S187), L173 (≠ T208), G174 (= G209), S176 (= S211), W306 (≠ Y342), F338 (≠ Y375)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
29% identity, 86% coverage: 50:498/521 of query aligns to 62:450/605 of Q936X2
- K91 (= K79) mutation to A: Loss of activity.
- S165 (= S191) mutation to A: Loss of activity.
- S189 (= S211) mutation to A: Loss of activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
28% identity, 86% coverage: 56:501/521 of query aligns to 51:430/461 of 4gysB
- active site: K72 (= K79), S146 (= S187), S147 (= S188), T165 (= T206), T167 (= T208), A168 (≠ G209), G169 (= G210), S170 (= S211), V173 (≠ Q214)
- binding malonate ion: A120 (= A128), G122 (= G130), S146 (= S187), T167 (= T208), A168 (≠ G209), S170 (= S211), S193 (≠ W234), G194 (= G235), V195 (≠ I236), R200 (≠ S241), Y297 (= Y357), R305 (≠ G363)
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
27% identity, 64% coverage: 3:333/521 of query aligns to 1:341/564 of 6te4A
Sites not aligning to the query:
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
28% identity, 56% coverage: 3:296/521 of query aligns to 2:259/482 of 3a2qA
- active site: K69 (= K79), S147 (= S187), S148 (= S188), N166 (≠ T206), A168 (≠ T208), A169 (≠ G209), G170 (= G210), A171 (≠ S211), I174 (≠ Q214)
- binding 6-aminohexanoic acid: G121 (≠ A128), G121 (≠ A128), N122 (≠ M129), S147 (= S187), A168 (≠ T208), A168 (≠ T208), A169 (≠ G209), A171 (≠ S211)
Sites not aligning to the query:
Query Sequence
>WP_013531785.1 NCBI__GCF_000185905.1:WP_013531785.1
MSDLTQLTISQARAKLHGKEITATEITEAYLSAIDRANPALNAYVAVTGDKARDMAKASD
ARLVKGEGGALEGIPLGIKDLFGTEGVHTQACSHVLDGFKPRYESTVTSNLWADGAVMLG
KLNMDEFAMGSSNETSYYGPVINPWRRSRLDTVVMPTTHQGDGGFVSAGGTRTARSLDNA
QLVPGGSSGGSATAVSAFLCAGATATDTGGSIRQPAAFTGTVGIKPTYGRCSRWGIVAFA
SSLDQAGPIARDVRDAAILLKSMASVDPKDTTSVDMPVPDYEAAIGKPIKGMKVGIPREY
RVEGMPEEIEALWQKGIAWLKDAGAEIVDISLPHTKYALPAYYIVAPAEASSNLARYDGV
RYGLRVPGKDIVDMYEKTRAAGFGREVKRRIMIGTYVLSAGYYDAYYLQAQKVRNLIKRD
FETVFAAGVDVILTPATPSAAFGIADEDMAADPVKMYLNDIFTVTVNMAGLPGIAVPAGL
DAKGLPLGLQLIGRPFDEETLFQTAAIIEQAAGTFQPEKWW
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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