SitesBLAST
Comparing BPHYT_RS09910 FitnessBrowser__BFirm:BPHYT_RS09910 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)
Q59118 Histamine oxidase; Copper amine oxidase; EC 1.4.3.22 from Arthrobacter globiformis (see paper)
45% identity, 96% coverage: 5:641/661 of query aligns to 19:647/684 of Q59118
- Y402 (= Y395) modified: 2',4',5'-topaquinone
P46881 Phenylethylamine oxidase; Primary amine oxidase; EC 1.4.3.21 from Arthrobacter globiformis (see paper)
43% identity, 95% coverage: 15:641/661 of query aligns to 11:627/638 of P46881
- C317 (= C330) modified: Disulfide link with 343
- C343 (= C356) modified: Disulfide link with 317
- Y382 (= Y395) modified: 2',4',5'-topaquinone
- H431 (= H445) binding
- H433 (= H447) binding
- H592 (= H606) binding
5zpnA Copper amine oxidase from arthrobacter globiformis anaerobically reduced by phenylethylamine at ph 8 at 288 k (1) (see paper)
43% identity, 95% coverage: 15:641/661 of query aligns to 3:619/620 of 5zpnA
- active site: Y276 (= Y297), D290 (= D311), Y374 (= Y395), H423 (= H445), H425 (= H447), H584 (= H606)
- binding copper (ii) ion: H423 (= H445), H425 (= H447), H584 (= H606)
- binding phenylacetaldehyde: L129 (≠ F151), Y288 (≠ A309), D290 (= D311), Y294 (= Y315), I371 (≠ V392), G372 (= G393), Y374 (= Y395)
3x3xA Copper amine oxidase from arthrobacter globiformis anaerobically reduced by phenylethylamine (see paper)
43% identity, 95% coverage: 15:641/661 of query aligns to 3:619/620 of 3x3xA
- active site: Y276 (= Y297), D290 (= D311), Y374 (= Y395), H423 (= H445), H425 (= H447), H584 (= H606)
- binding copper (ii) ion: H423 (= H445), H425 (= H447), H584 (= H606)
- binding glycerol: I31 (≠ F43), Y33 (≠ M45), V243 (≠ P264), S321 (≠ A342), D322 (= D343), R362 (= R383), E389 (≠ Q410), E391 (= E412)
- binding 2-phenyl-ethanol: P128 (= P150), L129 (≠ F151), Y288 (≠ A309), D290 (= D311), Y294 (= Y315), I371 (≠ V392), G372 (= G393), N373 (= N394)
2cg1A Agao in complex with wc11b (ru-wire inhibitor, 11-carbon linker, data set b) (see paper)
43% identity, 95% coverage: 15:641/661 of query aligns to 3:619/620 of 2cg1A
- active site: Y276 (= Y297), D290 (= D311), Y374 (= Y395), H423 (= H445), H425 (= H447), H584 (= H606)
- binding ruthenium wire, 11 carbon linker: F97 (= F116), P128 (= P150), L129 (≠ F151), Y288 (≠ A309), Y294 (= Y315), Y299 (≠ L320), T370 (= T391), G372 (= G393), Y374 (= Y395)
- binding copper (ii) ion: H423 (= H445), H425 (= H447), H584 (= H606)
2cg0A Agao in complex with wc9a (ru-wire inhibitor, 9-carbon linker, data set a) (see paper)
43% identity, 95% coverage: 15:641/661 of query aligns to 3:619/620 of 2cg0A
- active site: Y276 (= Y297), D290 (= D311), Y374 (= Y395), H423 (= H445), H425 (= H447), H584 (= H606)
- binding copper (ii) ion: H423 (= H445), H425 (= H447), H584 (= H606)
- binding ruthenium wire, 9 carbon linker: F97 (= F116), L129 (≠ F151), Y288 (≠ A309), Y294 (= Y315), Y299 (≠ L320), G372 (= G393), Y374 (= Y395)
2cfwA Agao in complex with wc7a (ru-wire inhibitor, 7-carbon linker, data set a) (see paper)
43% identity, 95% coverage: 15:641/661 of query aligns to 3:619/620 of 2cfwA
- active site: Y276 (= Y297), D290 (= D311), Y374 (= Y395), H423 (= H445), H425 (= H447), H584 (= H606)
- binding copper (ii) ion: H423 (= H445), H425 (= H447), H584 (= H606)
- binding ruthenium wire, 7 carbon linker: F97 (= F116), P128 (= P150), L129 (≠ F151), Y288 (≠ A309), Y294 (= Y315), Y299 (≠ L320), A300 (= A321), G372 (= G393), Y374 (= Y395)
2cflA Agao in complex with wc6b (ru-wire inhibitor, 6-carbon linker, data set b) (see paper)
43% identity, 95% coverage: 15:641/661 of query aligns to 3:619/620 of 2cflA
- active site: Y276 (= Y297), D290 (= D311), Y374 (= Y395), H423 (= H445), H425 (= H447), H584 (= H606)
- binding copper (ii) ion: H423 (= H445), H425 (= H447), H584 (= H606)
- binding ruthenium wire, 6 carbon linker: E94 (≠ I113), F97 (= F116), L129 (≠ F151), Y288 (≠ A309), Y294 (= Y315), G372 (= G393), Y374 (= Y395)
2cfkA Agao in complex with wc5 (ru-wire inhibitor, 5-carbon linker) (see paper)
43% identity, 95% coverage: 15:641/661 of query aligns to 3:619/620 of 2cfkA
- active site: Y276 (= Y297), D290 (= D311), Y374 (= Y395), H423 (= H445), H425 (= H447), H584 (= H606)
- binding copper (ii) ion: H423 (= H445), H425 (= H447), H584 (= H606)
- binding ruthenium wire, 5 carbon linker: E94 (≠ I113), F97 (= F116), P128 (= P150), L129 (≠ F151), Y288 (≠ A309), Y294 (= Y315), Y299 (≠ L320), T370 (= T391), G372 (= G393), Y374 (= Y395)
- binding ruthenium wire wc5: E94 (≠ I113), F97 (= F116), E98 (≠ M117), P128 (= P150), L129 (≠ F151), Y288 (≠ A309), Y294 (= Y315), R328 (≠ F349), G372 (= G393), Y374 (= Y395)
2bt3A Agao in complex with ruthenium-c4-wire at 1.73 angstroms (see paper)
43% identity, 95% coverage: 15:641/661 of query aligns to 3:619/620 of 2bt3A
- active site: Y276 (= Y297), D290 (= D311), Y374 (= Y395), H423 (= H445), H425 (= H447), H584 (= H606)
- binding copper (ii) ion: H423 (= H445), H425 (= H447), H584 (= H606)
- binding bis[1h,1'h-2,2'-bipyridinato(2-)-kappa~2~n~1~,n~1'~]{3-[4-(1,10-dihydro-1,10-phenanthrolin-4-yl-kappa~2~n~1~,n~10~)butoxy]-n,n-dimethylanilinato(2-)}ruthenium: E94 (≠ I113), F97 (= F116), P128 (= P150), L129 (≠ F151), Y288 (≠ A309), Y294 (= Y315), Q298 (≠ K319), Y299 (≠ L320), R328 (≠ F349), G372 (= G393), Y374 (= Y395)
1rjoA Agao + xe (see paper)
43% identity, 95% coverage: 15:641/661 of query aligns to 3:619/620 of 1rjoA
- active site: Y276 (= Y297), D290 (= D311), Y374 (= Y395), H423 (= H445), H425 (= H447), H584 (= H606)
- binding copper (ii) ion: H423 (= H445), H425 (= H447), H584 (= H606)
- binding xenon: I12 (≠ M24), V15 (≠ A27), Q16 (≠ C28), I31 (≠ F43), L34 (≠ V46), R63 (≠ T81), L82 (≠ F101), D83 (≠ G102), I230 (≠ V251), W232 (= W253), W235 (= W256), L237 (≠ F258), G325 (= G346), M363 (≠ L384), I365 (= I386), W380 (= W401), Y381 (= Y402), L382 (= L403), A392 (≠ C413), A394 (≠ L415), F427 (= F449), L582 (≠ H604)
1iqxA Crystal structure of cobalt-substituted amine oxidase from arthrobacter globiformis (see paper)
43% identity, 95% coverage: 15:641/661 of query aligns to 3:619/620 of 1iqxA
3wa2X High resolution crystal structure of copper amine oxidase from arthrobacter globiformis (see paper)
43% identity, 95% coverage: 15:641/661 of query aligns to 3:619/621 of 3wa2X
- binding copper (ii) ion: H423 (= H445), H425 (= H447), H584 (= H606)
- binding 1,2-ethanediol: Y33 (≠ M45), G35 (≠ E47), V36 (≠ L48), L37 (≠ R49), R53 (≠ V71), R109 (≠ A128), R180 (≠ E202), V181 (≠ L203), D242 (≠ T263), W341 (≠ Y362), I343 (≠ T364), N355 (≠ F376), Y356 (≠ E377), R358 (= R379), N360 (≠ S381), E405 (≠ W432), G407 (= G434), Q450 (≠ R472), P454 (≠ E476), G455 (≠ N477), G455 (≠ N477), E457 (≠ P479), R524 (≠ Q546), A527 (≠ G549), R543 (= R565), Y544 (= Y566), G556 (= G578)
- binding oxygen molecule: L148 (≠ V170), A149 (≠ S171), V164 (≠ I186), L167 (≠ V189), E391 (= E412), H509 (≠ N531), T513 (≠ L535), L514 (≠ M536), T530 (= T552)
8j6gA Neutron structure of copper amine oxidase from arthrobacter globiformis anaerobically reduced by phenylethylamine at pd 9.0
43% identity, 95% coverage: 15:641/661 of query aligns to 4:620/621 of 8j6gA
Q9P7F2 Copper amine oxidase 1; EC 1.4.3.21 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
37% identity, 97% coverage: 15:657/661 of query aligns to 25:678/712 of Q9P7F2
- H456 (≠ P443) mutation to A: Decreases copper amine oxidase activity.
- H458 (= H445) mutation to A: Impairs copper amine oxidase activity.
- H460 (= H447) mutation to A: Impairs copper amine oxidase activity.
- H627 (= H606) mutation to A: Impairs copper amine oxidase activity.
3sxxA Hansenula polymorpha copper amine oxidase-1 in complex with co(ii) (see paper)
36% identity, 99% coverage: 6:659/661 of query aligns to 1:665/666 of 3sxxA
3t0uB Hansenula polymorpha copper amine oxidase-1 in complex with cu(i) (see paper)
36% identity, 98% coverage: 12:659/661 of query aligns to 6:667/668 of 3t0uB
1a2vA Copper amine oxidase from hansenula polymorpha (see paper)
36% identity, 97% coverage: 12:654/661 of query aligns to 4:655/655 of 1a2vA
4ev5A Crystal structure of copper amine oxidase-1 from hansenula polymorpha in complex with benzylamine
36% identity, 97% coverage: 12:653/661 of query aligns to 4:654/654 of 4ev5A
- active site: Y288 (= Y297), D302 (= D311), Y388 (= Y395), H439 (= H445), H441 (= H447), H607 (= H606)
- binding benzylamine: W139 (≠ F151), A300 (= A309), D302 (= D311), Y306 (= Y315), A385 (≠ V392), A386 (≠ G393), Y388 (= Y395)
- binding copper (ii) ion: H439 (= H445), H441 (= H447), H607 (= H606)
4ev2A Crystal structure of copper amine oxidase-1 from hansenula polymorpha in complex with ethylamine
36% identity, 97% coverage: 12:653/661 of query aligns to 4:654/654 of 4ev2A
Query Sequence
>BPHYT_RS09910 FitnessBrowser__BFirm:BPHYT_RS09910
MNTNATTAAHAPFHPLDPLSGAEMQLACDLVKAAEKLDSHARFPMVELREPPKAEVVAFK
TGEYFSRTAFVLAIDRTNGATIEFEVDLREKKIAARRVMPFGEAPYGQPPIMIDDFMNAE
QIVKSDEAWRVAVMKRGLSEKDLERVQVDPFSAGCFDRENENGRRLVRCVSYYRETLTDN
GYAHPIEGVMAVVDLLEKKVIELVDDGRIIPIPRAKHNYDTPSLGEPRSTLKPLSIDQPD
GPSFTIDGWHVNWQNWNFRVGFTPREGLVLHQLSWDDGKSTRPIIYRASVTEMCVPYSDP
TTNHYWKSAFDAGEYGLGKLANQLELGCDCLGTIRYFDIPSADDFGNPFVMKNAVCMHEE
DYGTLWKHYEFRTGVFEMRRSRRLVISFFATVGNYDYGFYWYLYQDGTIQLECKLTGIVQ
TSAVADGDTYPWGGMITENLGGPTHQHFFNARMHMMVDGERNTVTEHEFVPRPMGENNPY
GNVFDTTKRVLKTESEAARNANGSTGRYWKVSNPNVKNAVGANPGYKLVVNDSPLMLADE
RSKVRQRGGFATRHVWVTPFDPAERYASGDYPNQHSGGDGLPRYIEANRNIENEDVVLWH
SFGHTHVCKPEDFPVMPVEYAGFMLKPNNFFSANPTMDLPAERDLNSVEDGKSTDHGCCK
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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