SitesBLAST
Comparing SMa2363 FitnessBrowser__Smeli:SMa2363 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)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
31% identity, 96% coverage: 4:455/471 of query aligns to 6:468/482 of 3a2qA
- active site: K69 (= K78), S147 (= S155), S148 (= S156), N166 (≠ T174), A168 (= A176), A169 (≠ G177), G170 (= G178), A171 (≠ S179), I174 (≠ V182)
- binding 6-aminohexanoic acid: G121 (= G129), G121 (= G129), N122 (≠ L130), S147 (= S155), A168 (= A176), A168 (= A176), A169 (≠ G177), A171 (≠ S179), C313 (≠ I312)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
27% identity, 86% coverage: 52:456/471 of query aligns to 179:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (= G129), T258 (≠ L132), S281 (= S155), G302 (≠ A176), G303 (= G177), S305 (= S179), S472 (= S330), I532 (≠ L397), M539 (≠ A406)
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, 86% coverage: 52:456/471 of query aligns to 179:589/607 of Q7XJJ7
- K205 (= K78) mutation to A: Loss of activity.
- SS 281:282 (= SS 155:156) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ AGGS 176:179) binding
- S305 (= S179) mutation to A: Loss of activity.
- R307 (= R181) mutation to A: Loss of activity.
- S360 (≠ R235) mutation to A: No effect.
3kfuE Crystal structure of the transamidosome (see paper)
32% identity, 80% coverage: 77:455/471 of query aligns to 50:454/468 of 3kfuE
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
29% identity, 76% coverage: 69:425/471 of query aligns to 68:423/457 of 5h6sC
- active site: K77 (= K78), S152 (= S155), S153 (= S156), L173 (≠ A176), G174 (= G177), G175 (= G178), S176 (= S179)
- binding 4-oxidanylbenzohydrazide: C126 (≠ G129), R128 (≠ S131), W129 (≠ L132), S152 (= S155), L173 (≠ A176), G174 (= G177), S176 (= S179), W306 (≠ S300), F338 (≠ N339)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
24% identity, 98% coverage: 6:465/471 of query aligns to 8:470/478 of 3h0mA
- active site: K72 (= K78), S147 (= S155), S148 (= S156), S166 (≠ T174), T168 (≠ A176), G169 (= G177), G170 (= G178), S171 (= S179), Q174 (≠ V182)
- binding glutamine: M122 (≠ L130), G123 (≠ S131), D167 (= D175), T168 (≠ A176), G169 (= G177), G170 (= G178), S171 (= S179), F199 (= F205), Y302 (≠ S304), R351 (≠ G341), D418 (≠ R401)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
24% identity, 98% coverage: 6:465/471 of query aligns to 8:470/478 of 3h0lA
- active site: K72 (= K78), S147 (= S155), S148 (= S156), S166 (≠ T174), T168 (≠ A176), G169 (= G177), G170 (= G178), S171 (= S179), Q174 (≠ V182)
- binding asparagine: G123 (≠ S131), S147 (= S155), G169 (= G177), G170 (= G178), S171 (= S179), Y302 (≠ S304), R351 (≠ G341), D418 (≠ R401)
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)
25% identity, 77% coverage: 94:454/471 of query aligns to 52:421/425 of Q9FR37
- S113 (= S155) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S156) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D175) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S179) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C187) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (≠ E283) mutation to T: Slightly reduces catalytic activity.
Sites not aligning to the query:
- 36 active site, Charge relay system; K→A: Loss of catalytic activity.; K→R: Reduces catalytic activity 10-fold.
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
28% identity, 97% coverage: 4:459/471 of query aligns to 7:480/487 of 1m21A
- active site: K81 (= K78), S160 (= S155), S161 (= S156), T179 (= T174), T181 (≠ A176), D182 (≠ G177), G183 (= G178), S184 (= S179), C187 (≠ V182)
- binding : A129 (vs. gap), N130 (vs. gap), F131 (vs. gap), C158 (≠ G153), G159 (= G154), S160 (= S155), S184 (= S179), C187 (≠ V182), I212 (≠ P203), R318 (vs. gap), L321 (vs. gap), L365 (≠ R332), F426 (≠ I395)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
28% identity, 89% coverage: 38:457/471 of query aligns to 32:475/485 of 2f2aA
- active site: K79 (= K78), S154 (= S155), S155 (= S156), S173 (≠ T174), T175 (≠ A176), G176 (= G177), G177 (= G178), S178 (= S179), Q181 (≠ V182)
- binding glutamine: G130 (≠ S131), S154 (= S155), D174 (= D175), T175 (≠ A176), G176 (= G177), S178 (= S179), F206 (≠ I212), Y309 (= Y293), Y310 (≠ W294), R358 (vs. gap), D425 (≠ A406)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
28% identity, 89% coverage: 38:457/471 of query aligns to 32:475/485 of 2dqnA
- active site: K79 (= K78), S154 (= S155), S155 (= S156), S173 (≠ T174), T175 (≠ A176), G176 (= G177), G177 (= G178), S178 (= S179), Q181 (≠ V182)
- binding asparagine: M129 (≠ L130), G130 (≠ S131), T175 (≠ A176), G176 (= G177), S178 (= S179), Y309 (= Y293), Y310 (≠ W294), R358 (vs. gap), D425 (≠ A406)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
32% identity, 48% coverage: 10:234/471 of query aligns to 8:228/457 of 6c6gA
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
26% identity, 89% coverage: 50:466/471 of query aligns to 51:484/490 of 4yjiA
- active site: K79 (= K78), S158 (= S155), S159 (= S156), G179 (≠ A176), G180 (= G177), G181 (= G178), A182 (≠ S179)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L80), G132 (= G129), S158 (= S155), G179 (≠ A176), G180 (= G177), A182 (≠ S179)
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)
29% identity, 61% coverage: 7:292/471 of query aligns to 81:363/579 of Q9TUI8
- S217 (= S155) mutation to A: Loss of activity.
- S218 (= S156) mutation to A: Lowers activity by at least 98%.
- D237 (= D175) mutation D->E,N: Loss of activity.
- S241 (= S179) mutation to A: Loss of activity.
- C249 (= C187) mutation to A: Loss of activity.
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
33% identity, 48% coverage: 85:309/471 of query aligns to 101:338/508 of 3a1iA
- active site: S170 (= S155), S171 (= S156), G189 (≠ T174), Q191 (≠ A176), G192 (= G177), G193 (= G178), A194 (≠ S179), I197 (≠ V182)
- binding benzamide: F145 (≠ L130), S146 (= S131), G147 (≠ L132), Q191 (≠ A176), G192 (= G177), G193 (= G178), A194 (≠ S179), W327 (vs. gap)
Sites not aligning to the query:
3qkvA Crystal structure of fatty acid amide hydrolase with small molecule compound (see paper)
28% identity, 70% coverage: 105:433/471 of query aligns to 139:494/549 of 3qkvA
- active site: S189 (= S155), S190 (= S156), T208 (= T174), I210 (≠ A176), G211 (= G177), G212 (= G178), S213 (= S179), F216 (≠ V182)
- binding (6-bromo-1'H,4H-spiro[1,3-benzodioxine-2,4'-piperidin]-1'-yl)methanol: L164 (= L130), S165 (= S131), I210 (≠ A176), G211 (= G177), S213 (= S179), T460 (= T403), I463 (≠ A406)
Sites not aligning to the query:
3qk5A Crystal structure of fatty acid amide hydrolase with small molecule inhibitor (see paper)
28% identity, 70% coverage: 105:433/471 of query aligns to 139:494/549 of 3qk5A
- active site: S189 (= S155), S190 (= S156), T208 (= T174), I210 (≠ A176), G211 (= G177), G212 (= G178), S213 (= S179), F216 (≠ V182)
- binding (3-{(3R)-1-[4-(1-benzothiophen-2-yl)pyrimidin-2-yl]piperidin-3-yl}-2-methyl-1H-pyrrolo[2,3-b]pyridin-1-yl)acetonitrile: L164 (= L130), S165 (= S131), I210 (≠ A176), G211 (= G177), G212 (= G178), S213 (= S179), F216 (≠ V182), L376 (≠ A327), I379 (≠ S330), M408 (≠ G341), G457 (vs. gap), T460 (= T403), I463 (≠ A406)
Sites not aligning to the query:
3qj9A Crystal structure of fatty acid amide hydrolase with small molecule inhibitor (see paper)
28% identity, 70% coverage: 105:433/471 of query aligns to 139:494/549 of 3qj9A
- active site: S189 (= S155), S190 (= S156), T208 (= T174), I210 (≠ A176), G211 (= G177), G212 (= G178), S213 (= S179), F216 (≠ V182)
- binding 1-{(3S)-1-[4-(1-benzofuran-2-yl)pyrimidin-2-yl]piperidin-3-yl}-3-ethyl-1,3-dihydro-2H-benzimidazol-2-one: L164 (= L130), S165 (= S131), F166 (≠ L132), I210 (≠ A176), L376 (≠ A327), I379 (≠ S330), L401 (vs. gap), M408 (≠ G341), G457 (vs. gap), T460 (= T403), I463 (≠ A406)
Sites not aligning to the query:
3ppmA Crystal structure of a noncovalently bound alpha-ketoheterocycle inhibitor (phenhexyl/oxadiazole/pyridine) to a humanized variant of fatty acid amide hydrolase (see paper)
28% identity, 70% coverage: 105:433/471 of query aligns to 135:490/546 of 3ppmA
- active site: S185 (= S155), S186 (= S156), T204 (= T174), I206 (≠ A176), G207 (= G177), G208 (= G178), S209 (= S179), F212 (≠ V182)
- binding fluoride ion: D205 (= D175), I206 (≠ A176), G207 (= G177), S209 (= S179)
- binding 7-phenyl-1-[5-(pyridin-2-yl)-1,3,4-oxadiazol-2-yl]heptan-1-one: M159 (≠ G129), F160 (≠ L130), S185 (= S155), T204 (= T174), I206 (≠ A176), S209 (= S179), G236 (= G206), L246 (= L216), T456 (= T403), M463 (≠ A410)
Sites not aligning to the query:
3k84A Crystal structure analysis of a oleyl/oxadiazole/pyridine inhibitor bound to a humanized variant of fatty acid amide hydrolase (see paper)
28% identity, 70% coverage: 105:433/471 of query aligns to 135:490/546 of 3k84A
- active site: S185 (= S155), S186 (= S156), T204 (= T174), I206 (≠ A176), G207 (= G177), G208 (= G178), S209 (= S179), F212 (≠ V182)
- binding (9Z)-1-(5-pyridin-2-yl-1,3,4-oxadiazol-2-yl)octadec-9-en-1-one: M159 (≠ G129), F160 (≠ L130), S161 (= S131), S185 (= S155), T204 (= T174), I206 (≠ A176), G207 (= G177), S209 (= S179), T345 (≠ S304), T456 (= T403)
Sites not aligning to the query:
Query Sequence
>SMa2363 FitnessBrowser__Smeli:SMa2363
MAGDATSLGQAIQMGRLTASEAMEASLAAACQLAETGAIVHVDPTLGRTAAENADARLRH
LPGGGRIPPFLGVPSLAKDLGGPFAGLSVAAGSNMLERRAAVAEDSDLAERLRGTGLCFF
GLTTVPEMGLSLASEPAAGPICRNPLDAGRTPGGSSGGAAAAVAAGIVAIAHATDAGGSM
RVPAACCGLFGLKASRGAIAAGPSFGNHLGGIASELALCRSVRDLAVIFNAAAGRARGPF
ADPWFAPSPPGPLRVGLLLETGDQYPTEPARSEAVEEAARALEADGHSVVPMYWDAFAAS
VATSGRALRDIIAVNLANFVVSAGLDAGRSERLTQAFINHGSQLEATALWATLGDAVHAS
HAVWSLFDRVDCILTPMLASAPLPIGSFPFDHDDIDLQIRRMTAFAPLAALANATGFPAL
TLPFGADDAGLPLPVQILAPMGGDRLLIELAARLEREGRWQHRFAVAGIPE
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