SitesBLAST
Comparing GFF1992 FitnessBrowser__Phaeo:GFF1992 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)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
33% identity, 99% coverage: 4:473/474 of query aligns to 3:456/457 of 5h6sC
- active site: K77 (= K76), S152 (= S151), S153 (= S152), L173 (≠ M172), G174 (≠ M173), G175 (= G174), S176 (= S175)
- binding 4-oxidanylbenzohydrazide: C126 (≠ G125), R128 (≠ G127), W129 (≠ S128), S152 (= S151), L173 (≠ M172), G174 (≠ M173), S176 (= S175), W306 (= W308), F338 (≠ S333)
3kfuE Crystal structure of the transamidosome (see paper)
34% identity, 95% coverage: 8:457/474 of query aligns to 2:457/468 of 3kfuE
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
28% identity, 96% coverage: 1:454/474 of query aligns to 1:473/485 of 2f2aA
- active site: K79 (= K76), S154 (= S151), S155 (= S152), S173 (= S170), T175 (≠ M172), G176 (≠ M173), G177 (= G174), S178 (= S175), Q181 (≠ N178)
- binding glutamine: G130 (= G127), S154 (= S151), D174 (= D171), T175 (≠ M172), G176 (≠ M173), S178 (= S175), F206 (= F204), Y309 (≠ W308), Y310 (≠ S309), R358 (vs. gap), D425 (vs. gap)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
28% identity, 96% coverage: 1:454/474 of query aligns to 1:473/485 of 2dqnA
- active site: K79 (= K76), S154 (= S151), S155 (= S152), S173 (= S170), T175 (≠ M172), G176 (≠ M173), G177 (= G174), S178 (= S175), Q181 (≠ N178)
- binding asparagine: M129 (≠ L126), G130 (= G127), T175 (≠ M172), G176 (≠ M173), S178 (= S175), Y309 (≠ W308), Y310 (≠ S309), R358 (vs. gap), D425 (vs. gap)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
28% identity, 96% coverage: 7:461/474 of query aligns to 7:480/490 of 4yjiA
- active site: K79 (= K76), S158 (= S151), S159 (= S152), G179 (≠ M172), G180 (≠ M173), G181 (= G174), A182 (≠ S175)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L78), G132 (= G125), S158 (= S151), G179 (≠ M172), G180 (≠ M173), A182 (≠ S175)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
33% identity, 91% coverage: 10:439/474 of query aligns to 5:433/457 of 6c6gA
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
29% identity, 95% coverage: 13:464/474 of query aligns to 12:478/482 of 3a2qA
- active site: K69 (= K76), S147 (= S151), S148 (= S152), N166 (≠ S170), A168 (≠ M172), A169 (≠ M173), G170 (= G174), A171 (≠ S175), I174 (≠ N178)
- binding 6-aminohexanoic acid: G121 (= G125), G121 (= G125), N122 (≠ L126), S147 (= S151), A168 (≠ M172), A168 (≠ M172), A169 (≠ M173), A171 (≠ S175), C313 (≠ R312)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 83% coverage: 67:459/474 of query aligns to 63:469/478 of 3h0mA
- active site: K72 (= K76), S147 (= S151), S148 (= S152), S166 (= S170), T168 (≠ M172), G169 (≠ M173), G170 (= G174), S171 (= S175), Q174 (≠ N178)
- binding glutamine: M122 (≠ L126), G123 (= G127), D167 (= D171), T168 (≠ M172), G169 (≠ M173), G170 (= G174), S171 (= S175), F199 (= F204), Y302 (≠ S307), R351 (vs. gap), D418 (vs. gap)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 83% coverage: 67:459/474 of query aligns to 63:469/478 of 3h0lA
- active site: K72 (= K76), S147 (= S151), S148 (= S152), S166 (= S170), T168 (≠ M172), G169 (≠ M173), G170 (= G174), S171 (= S175), Q174 (≠ N178)
- binding asparagine: G123 (= G127), S147 (= S151), G169 (≠ M173), G170 (= G174), S171 (= S175), Y302 (≠ S307), R351 (vs. gap), D418 (vs. gap)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
30% identity, 82% coverage: 63:453/474 of query aligns to 82:496/508 of 3a1iA
- active site: K95 (= K76), S170 (= S151), S171 (= S152), G189 (≠ S170), Q191 (≠ M172), G192 (≠ M173), G193 (= G174), A194 (≠ S175), I197 (≠ N178)
- binding benzamide: F145 (≠ L126), S146 (≠ G127), G147 (≠ S128), Q191 (≠ M172), G192 (≠ M173), G193 (= G174), A194 (≠ S175), W327 (≠ A317)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
32% identity, 96% coverage: 12:466/474 of query aligns to 11:486/487 of 1m21A
- active site: K81 (= K76), S160 (= S151), S161 (= S152), T179 (≠ S170), T181 (≠ M172), D182 (≠ M173), G183 (= G174), S184 (= S175), C187 (≠ N178)
- binding : A129 (≠ G125), N130 (vs. gap), F131 (vs. gap), C158 (≠ G149), G159 (= G150), S160 (= S151), S184 (= S175), C187 (≠ N178), I212 (≠ L208), R318 (≠ S309), L321 (≠ R312), L365 (≠ I349), F426 (≠ Y389)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
27% identity, 82% coverage: 48:437/474 of query aligns to 173:571/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (= G125), T258 (≠ S128), S281 (= S151), G302 (≠ M172), G303 (≠ M173), S305 (= S175), S472 (≠ E337), I532 (≠ M398), M539 (= M405)
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)
27% identity, 82% coverage: 48:437/474 of query aligns to 173:571/607 of Q7XJJ7
- K205 (= K76) mutation to A: Loss of activity.
- SS 281:282 (= SS 151:152) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ MMGS 172:175) binding
- S305 (= S175) mutation to A: Loss of activity.
- R307 (= R177) mutation to A: Loss of activity.
- S360 (= S231) mutation to A: No effect.
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
27% identity, 91% coverage: 19:451/474 of query aligns to 41:484/507 of Q84DC4
- K100 (= K76) mutation to A: Abolishes activity on mandelamide.
- S180 (= S151) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S152) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ M173) 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 (= S175) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ N178) 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 (vs. gap) 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 (vs. gap) 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 (≠ M405) 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.
Sites not aligning to the query:
- 31 T→I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
37% identity, 49% coverage: 4:233/474 of query aligns to 3:241/564 of 6te4A
Sites not aligning to the query:
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
29% identity, 87% coverage: 44:454/474 of query aligns to 39:438/461 of 4gysB
- active site: K72 (= K76), S146 (= S151), S147 (= S152), T165 (≠ S170), T167 (≠ M172), A168 (≠ M173), G169 (= G174), S170 (= S175), V173 (≠ N178)
- binding malonate ion: A120 (≠ G125), G122 (= G127), S146 (= S151), T167 (≠ M172), A168 (≠ M173), S170 (= S175), S193 (≠ N211), G194 (= G212), V195 (≠ P213), R200 (≠ P218), Y297 (≠ W305), R305 (≠ G319)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
26% identity, 86% coverage: 41:448/474 of query aligns to 26:401/412 of 1o9oA
- active site: K62 (= K76), A131 (≠ S151), S132 (= S152), T150 (≠ S170), T152 (≠ M172), G153 (≠ M173), G154 (= G174), S155 (= S175), R158 (≠ N178)
- binding 3-amino-3-oxopropanoic acid: G130 (= G150), T152 (≠ M172), G153 (≠ M173), G154 (= G174), S155 (= S175), R158 (≠ N178), P359 (≠ D399)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
26% identity, 86% coverage: 41:448/474 of query aligns to 26:401/412 of 1ocmA
- active site: K62 (= K76), S131 (= S151), S132 (= S152), T152 (≠ M172), G153 (≠ M173), G154 (= G174), S155 (= S175)
- binding pyrophosphate 2-: R113 (≠ G127), S131 (= S151), Q151 (≠ D171), T152 (≠ M172), G153 (≠ M173), G154 (= G174), S155 (= S175), R158 (≠ N178), P359 (≠ D399)
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)
31% identity, 61% coverage: 10:297/474 of query aligns to 81:362/579 of Q9TUI8
- S217 (= S151) mutation to A: Loss of activity.
- S218 (= S152) mutation to A: Lowers activity by at least 98%.
- D237 (= D171) mutation D->E,N: Loss of activity.
- S241 (= S175) mutation to A: Loss of activity.
- C249 (= C183) mutation to A: Loss of activity.
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)
30% identity, 39% coverage: 12:195/474 of query aligns to 83:261/579 of P97612
- K142 (= K76) mutation to A: Lowers activity 40000-fold. Lowers activity 70000-fold; when associated with A-217.
- S217 (= S151) mutation to A: Lowers activity 3000-fold. Lowers activity 70000-fold; when associated with A-142.
Query Sequence
>GFF1992 FitnessBrowser__Phaeo:GFF1992
MSETTPSARETLQAISAGRRTAVALMEETLARIDALNPSLNAIVALRDREVLLAEAAAAD
RSTTRGPLHGLPMAIKDLANVAGVRSTQGSPLLADFVPQQDDLMVARLRAAGALFIGKTN
TPEFGLGSHTFNPVHGATANPYDHSRSCGGSSGGAAVALATGMVALADGSDMMGSLRNPA
GWCNVYGFRPSWGRVPGEPRGDLFLHPLSTNGPMARCPEDLALLLDVMSGSDPRQPLAAT
AGAGRRVSPLPEARPMRIGWLADWGGAYPMETGILETCETALETLRTLGHQVETLAPPFA
AERIWQSWSTLRSFSVASGLRVFGGQMQQLKDSAQWELQSGLALSGQEIQAASDLRSDWQ
RVAARLFSQYDALVLPTAQCWPFDIALDYPQVIGETAMDSYHRWMEVVTPVSLIGVPCLA
APAGFGPAGLPMGIQIFAAHGRDRELLALGQQYHWATRWPERRPPQTPSTTAAR
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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