SitesBLAST
Comparing WP_011882484.1 NCBI__GCF_000016205.1:WP_011882484.1 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)
30% identity, 92% coverage: 22:477/493 of query aligns to 7:473/485 of 2f2aA
- active site: K79 (= K95), S154 (= S170), S155 (= S171), S173 (= S189), T175 (≠ F191), G176 (= G192), G177 (= G193), S178 (= S194), Q181 (≠ N197)
- binding glutamine: G130 (= G146), S154 (= S170), D174 (= D190), T175 (≠ F191), G176 (= G192), S178 (= S194), F206 (= F223), Y309 (≠ I324), Y310 (≠ W325), R358 (≠ L364), D425 (≠ Q420)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
30% identity, 92% coverage: 22:477/493 of query aligns to 7:473/485 of 2dqnA
- active site: K79 (= K95), S154 (= S170), S155 (= S171), S173 (= S189), T175 (≠ F191), G176 (= G192), G177 (= G193), S178 (= S194), Q181 (≠ N197)
- binding asparagine: M129 (≠ L145), G130 (= G146), T175 (≠ F191), G176 (= G192), S178 (= S194), Y309 (≠ I324), Y310 (≠ W325), R358 (≠ L364), D425 (≠ Q420)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
31% identity, 94% coverage: 18:478/493 of query aligns to 2:467/478 of 3h0mA
- active site: K72 (= K95), S147 (= S170), S148 (= S171), S166 (= S189), T168 (≠ F191), G169 (= G192), G170 (= G193), S171 (= S194), Q174 (≠ N197)
- binding glutamine: M122 (≠ L145), G123 (= G146), D167 (= D190), T168 (≠ F191), G169 (= G192), G170 (= G193), S171 (= S194), F199 (= F223), Y302 (≠ L327), R351 (vs. gap), D418 (= D422)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
31% identity, 94% coverage: 18:478/493 of query aligns to 2:467/478 of 3h0lA
- active site: K72 (= K95), S147 (= S170), S148 (= S171), S166 (= S189), T168 (≠ F191), G169 (= G192), G170 (= G193), S171 (= S194), Q174 (≠ N197)
- binding asparagine: G123 (= G146), S147 (= S170), G169 (= G192), G170 (= G193), S171 (= S194), Y302 (≠ L327), R351 (vs. gap), D418 (= D422)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
31% identity, 94% coverage: 20:480/493 of query aligns to 4:447/457 of 5h6sC
- active site: K77 (= K95), S152 (= S170), S153 (= S171), L173 (≠ F191), G174 (= G192), G175 (= G193), S176 (= S194)
- binding 4-oxidanylbenzohydrazide: C126 (≠ G144), R128 (≠ G146), W129 (≠ S147), S152 (= S170), L173 (≠ F191), G174 (= G192), S176 (= S194), W306 (vs. gap), F338 (≠ E356)
3kfuE Crystal structure of the transamidosome (see paper)
35% identity, 93% coverage: 23:479/493 of query aligns to 2:456/468 of 3kfuE
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
31% identity, 94% coverage: 22:482/493 of query aligns to 7:478/490 of 4yjiA
- active site: K79 (= K95), S158 (= S170), S159 (= S171), G179 (≠ F191), G180 (= G192), G181 (= G193), A182 (≠ S194)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L97), G132 (= G144), S158 (= S170), G179 (≠ F191), G180 (= G192), A182 (≠ S194)
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, 75% coverage: 111:480/493 of query aligns to 222:591/607 of Q7XJJ7
- SS 281:282 (= SS 170:171) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ FGGS 191:194) binding
- S305 (= S194) mutation to A: Loss of activity.
- R307 (= R196) mutation to A: Loss of activity.
- S360 (≠ Y250) mutation to A: No effect.
Sites not aligning to the query:
- 205 K→A: Loss of activity.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
30% identity, 75% coverage: 111:480/493 of query aligns to 222:591/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (= G144), T258 (≠ S147), S281 (= S170), G302 (≠ F191), G303 (= G192), S305 (= S194), S472 (≠ E360), I532 (= I416), M539 (= M428)
Sites not aligning to the query:
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
31% identity, 93% coverage: 27:486/493 of query aligns to 11:477/482 of 3a2qA
- active site: K69 (= K95), S147 (= S170), S148 (= S171), N166 (≠ S189), A168 (≠ F191), A169 (≠ G192), G170 (= G193), A171 (≠ S194), I174 (≠ N197)
- binding 6-aminohexanoic acid: G121 (= G144), G121 (= G144), N122 (≠ L145), S147 (= S170), A168 (≠ F191), A168 (≠ F191), A169 (≠ G192), A171 (≠ S194), C313 (≠ W325)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
31% identity, 80% coverage: 85:478/493 of query aligns to 85:498/508 of 3a1iA
- active site: K95 (= K95), S170 (= S170), S171 (= S171), G189 (≠ S189), Q191 (≠ F191), G192 (= G192), G193 (= G193), A194 (≠ S194), I197 (≠ N197)
- binding benzamide: F145 (≠ L145), S146 (≠ G146), G147 (≠ S147), Q191 (≠ F191), G192 (= G192), G193 (= G193), A194 (≠ S194), W327 (= W325)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
37% identity, 53% coverage: 25:284/493 of query aligns to 5:263/457 of 6c6gA
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
29% identity, 94% coverage: 16:478/493 of query aligns to 10:477/487 of 1m21A
- active site: K81 (= K95), S160 (= S170), S161 (= S171), T179 (≠ S189), T181 (≠ F191), D182 (≠ G192), G183 (= G193), S184 (= S194), C187 (≠ N197)
- binding : A129 (≠ G144), N130 (≠ S147), F131 (≠ H148), C158 (≠ G168), G159 (= G169), S160 (= S170), S184 (= S194), C187 (≠ N197), I212 (≠ V222), R318 (vs. gap), L321 (vs. gap), L365 (≠ A357), F426 (≠ M421)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
27% identity, 93% coverage: 20:478/493 of query aligns to 27:488/507 of Q84DC4
- T31 (≠ G24) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K95) mutation to A: Abolishes activity on mandelamide.
- S180 (= S170) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S171) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G192) 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 (= S194) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ N197) 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 (≠ G309) 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 (≠ S376) 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 (≠ M428) 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.
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
34% identity, 48% coverage: 18:253/493 of query aligns to 2:242/564 of 6te4A
Sites not aligning to the query:
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
30% identity, 88% coverage: 59:490/493 of query aligns to 39:445/461 of 4gysB
- active site: K72 (= K95), S146 (= S170), S147 (= S171), T165 (≠ S189), T167 (≠ F191), A168 (≠ G192), G169 (= G193), S170 (= S194), V173 (≠ N197)
- binding malonate ion: A120 (≠ G144), G122 (= G146), S146 (= S170), T167 (≠ F191), A168 (≠ G192), S170 (= S194), S193 (≠ W217), G194 (≠ P218), V195 (≠ A219), R200 (≠ Q225), Y297 (vs. gap), R305 (= R332)
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
34% identity, 36% coverage: 84:261/493 of query aligns to 27:206/450 of 4n0iA
- active site: K38 (= K95), S116 (= S170), S117 (= S171), T135 (≠ S189), T137 (≠ F191), G138 (= G192), G139 (= G193), S140 (= S194), L143 (≠ N197)
- binding glutamine: G89 (= G146), T137 (≠ F191), G138 (= G192), S140 (= S194), Y168 (≠ F223)
Sites not aligning to the query:
Q9TUI8 Fatty-acid amide hydrolase 1; Anandamide amidase; Anandamide amidohydrolase 1; Fatty acid ester hydrolase; Oleamide hydrolase 1; EC 3.5.1.99; EC 3.1.1.- from Sus scrofa (Pig) (see paper)
26% identity, 69% coverage: 18:359/493 of query aligns to 74:396/579 of Q9TUI8
- S217 (= S170) mutation to A: Loss of activity.
- S218 (= S171) mutation to A: Lowers activity by at least 98%.
- D237 (= D190) mutation D->E,N: Loss of activity.
- S241 (= S194) mutation to A: Loss of activity.
- C249 (= C202) mutation to A: Loss of activity.
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
35% identity, 38% coverage: 79:264/493 of query aligns to 46:224/412 of 1o9oA
- active site: K62 (= K95), A131 (≠ S170), S132 (= S171), T150 (≠ S189), T152 (≠ F191), G153 (= G192), G154 (= G193), S155 (= S194), R158 (≠ N197)
- binding 3-amino-3-oxopropanoic acid: G130 (= G169), T152 (≠ F191), G153 (= G192), G154 (= G193), S155 (= S194), R158 (≠ N197)
Sites not aligning to the query:
P97612 Fatty-acid amide hydrolase 1; Anandamide amidase; Anandamide amidohydrolase 1; Fatty acid ester hydrolase; Oleamide hydrolase 1; EC 3.5.1.99; EC 3.1.1.- from Rattus norvegicus (Rat) (see paper)
31% identity, 40% coverage: 43:237/493 of query aligns to 99:287/579 of P97612
- K142 (= K95) mutation to A: Lowers activity 40000-fold. Lowers activity 70000-fold; when associated with A-217.
- S217 (= S170) mutation to A: Lowers activity 3000-fold. Lowers activity 70000-fold; when associated with A-142.
Query Sequence
>WP_011882484.1 NCBI__GCF_000016205.1:WP_011882484.1
MPHGAPYLAPASIPVDPLVRLSAGELASAIRRKAVSCVETMRAYLDHIERVNGAVNALIS
LRDRATLLAEAAEKDAALARGEYHGWLHGMPQAPKDLAMTKGLRTTYGSPIFRDHVPQAD
SIGVGRMRAAGAIFIGKTNTPEFGLGSHTFNDVHGATRNPYDLTRSAGGSSGGSAAALAA
RMLPVADGSDFGGSLRNPAAFCNVYGMRPSQGRVPRWPAVDVFMQQLGTEGPMGRTVGDV
AQLLAIQAGYDANDPLSLAEQPLVFATPLDTDLRGRRIAWVGDWDGYLATEPGVLAQCEQ
GLATLREIGCDVDAALPAFAPERIWRLWLAHRHLLAGGGLLAHYRDPARRALLKPEAIYE
VEGLLAMGGAAVFDASVERTAWHQAVLRFFDRYDFIAAPSAQVFPFDVELRWPQAIAGRQ
MDTYHRWMETVVPWTLAGCPVISVPVGFNDDGLPMGMQLIGRPRADLAVLQLARGYEQAA
DWVGRRLPGWMAA
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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