SitesBLAST
Comparing 15508 FitnessBrowser__Keio:15508 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)
P46883 Primary amine oxidase; 2-phenylethylamine oxidase; Copper amine oxidase; Tyramine oxidase; EC 1.4.3.21 from Escherichia coli (strain K12) (see 6 papers)
100% identity, 100% coverage: 1:757/757 of query aligns to 1:757/757 of P46883
- 1:30 (vs. 1:30, 100% identical) signal peptide
- 411:422 (vs. 411:422, 100% identical) binding
- D413 (= D413) active site, Proton acceptor
- VGNYDY 493:498 (= VGNYDY 493:498) binding
- Y496 (= Y496) active site, Schiff-base intermediate with substrate; via topaquinone; modified: 2',4',5'-topaquinone
- H554 (= H554) binding
- H556 (= H556) binding
- D563 (= D563) binding
- L564 (= L564) binding
- D565 (= D565) binding
- E603 (= E603) binding
- Y697 (= Y697) binding
- D700 (= D700) binding
- E702 (= E702) binding
- D708 (= D708) binding
- A709 (= A709) binding
- H719 (= H719) binding
1oacB Crystal structure of a quinoenzyme: copper amine oxidase of escherichia coli at 2 angstroems resolution (see paper)
100% identity, 96% coverage: 35:757/757 of query aligns to 1:723/723 of 1oacB
- active site: Y365 (= Y399), D379 (= D413), Y462 (= Y496), H520 (= H554), H522 (= H556), H685 (= H719)
- binding calcium ion: D529 (= D563), L530 (= L564), D531 (= D565), E569 (= E603), Y663 (= Y697), D666 (= D700), E668 (= E702), D674 (= D708), A675 (= A709)
- binding copper (ii) ion: Y462 (= Y496), H520 (= H554), H522 (= H556), H685 (= H719)
2wgqA Zinc substituted e coli copper amine oxidase, a model for the precursor for 2,4,5-trihydroxyphenylalaninequinone formation
100% identity, 95% coverage: 35:754/757 of query aligns to 1:720/720 of 2wgqA
- active site: Y365 (= Y399), D379 (= D413), Y462 (= Y496), H520 (= H554), H522 (= H556), H685 (= H719)
- binding calcium ion: D529 (= D563), L530 (= L564), D531 (= D565), E569 (= E603), Y663 (= Y697), D666 (= D700), E668 (= E702), D674 (= D708), A675 (= A709)
- binding zinc ion: Y462 (= Y496), H520 (= H554), H522 (= H556), H685 (= H719)
2w0qA E. Coli copper amine oxidase in complex with xenon (see paper)
100% identity, 95% coverage: 37:754/757 of query aligns to 1:718/718 of 2w0qA
- active site: Y363 (= Y399), D377 (= D413), Y460 (= Y496), H518 (= H554), H520 (= H556), H683 (= H719)
- binding calcium ion: D527 (= D563), L528 (= L564), D529 (= D565), E567 (= E603), Y661 (= Y697), E666 (= E702), D672 (= D708), A673 (= A709)
- binding copper (ii) ion: H518 (= H554), H520 (= H556), H683 (= H719)
- binding xenon: V181 (= V217), L182 (= L218), L183 (= L219), F186 (= F222), M316 (= M352), D323 (= D359), F324 (= F360), T338 (= T374), Y375 (= Y411), Y381 (= Y417), Y381 (= Y417), S388 (= S424), I390 (= I426), A420 (= A456), W453 (= W489), I454 (= I490), G458 (= G494), L537 (= L573), P542 (= P578), V543 (= V579), M557 (= M593), A570 (= A606), Q572 (= Q608), I599 (= I635), L632 (= L668), L632 (= L668)
1d6yA Crystal structure of e. Coli copper-containing amine oxidase anaerobically reduced with beta-phenylethylamine and complexed with nitric oxide. (see paper)
100% identity, 95% coverage: 37:754/757 of query aligns to 1:718/718 of 1d6yA
- active site: Y363 (= Y399), D377 (= D413), Y460 (= Y496), H518 (= H554), H520 (= H556), H683 (= H719)
- binding calcium ion: D527 (= D563), L528 (= L564), D529 (= D565), E567 (= E603), H638 (= H674), Y661 (= Y697), D664 (= D700), D672 (= D708), A673 (= A709)
- binding copper (ii) ion: H518 (= H554), H520 (= H556), H683 (= H719)
- binding phenylacetaldehyde: T217 (= T253), P218 (= P254), L219 (= L255), Y375 (= Y411), Y381 (= Y417), G458 (= G494), Y460 (= Y496)
- binding nitric oxide: Y460 (= Y496), H518 (= H554)
- binding 2-phenylethylamine: D96 (= D132), Q100 (= Q136)
1d6uA Crystal structure of e. Coli amine oxidase anaerobically reduced with beta-phenylethylamine (see paper)
100% identity, 95% coverage: 37:754/757 of query aligns to 1:718/718 of 1d6uA
- active site: Y363 (= Y399), D377 (= D413), Y460 (= Y496), H518 (= H554), H520 (= H556), H683 (= H719)
- binding calcium ion: D527 (= D563), L528 (= L564), D529 (= D565), E567 (= E603), H638 (= H674), Y661 (= Y697), D664 (= D700), D672 (= D708), A673 (= A709)
- binding copper (ii) ion: H518 (= H554), H520 (= H556), H683 (= H719)
- binding phenylacetaldehyde: L219 (= L255), Y375 (= Y411), D377 (= D413), Y381 (= Y417), V457 (= V493), G458 (= G494), Y460 (= Y496)
- binding 2-phenylethylamine: D96 (= D132), Q100 (= Q136)
Q59118 Histamine oxidase; Copper amine oxidase; EC 1.4.3.22 from Arthrobacter globiformis (see paper)
31% identity, 83% coverage: 124:750/757 of query aligns to 28:643/684 of Q59118
- Y402 (= Y496) modified: 2',4',5'-topaquinone
1w2zA Psao and xenon (see paper)
30% identity, 83% coverage: 124:753/757 of query aligns to 3:632/642 of 1w2zA
- active site: Y281 (= Y399), D295 (= D413), Y382 (= Y496), H437 (= H554), H439 (= H556), H598 (= H719)
- binding copper (ii) ion: H437 (= H554), H439 (= H556), H598 (= H719)
- binding manganese (ii) ion: D446 (= D563), F447 (≠ L564), D448 (= D565), D587 (= D708), I588 (≠ A709)
- binding xenon: L402 (≠ A516), Y441 (= Y558), F447 (≠ L564), Y518 (= Y633), R519 (≠ Q634), L520 (≠ I635), M590 (≠ V711), T613 (≠ V734)
1ksiA Crystal structure of a eukaryotic (pea seedling) copper-containing amine oxidase at 2.2a resolution (see paper)
30% identity, 83% coverage: 124:753/757 of query aligns to 3:632/642 of 1ksiA
- active site: Y281 (= Y399), D295 (= D413), Y382 (= Y496), H437 (= H554), H439 (= H556), H598 (= H719)
- binding copper (ii) ion: H437 (= H554), H439 (= H556), H598 (= H719)
- binding manganese (ii) ion: D446 (= D563), F447 (≠ L564), D448 (= D565), D587 (= D708), I588 (≠ A709)
Q43077 Primary amine oxidase; Amine oxidase [copper-containing]; EC 1.4.3.21 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
30% identity, 83% coverage: 124:753/757 of query aligns to 33:662/674 of Q43077
- N156 (≠ D246) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- C162 (≠ T252) modified: Disulfide link with 183
- C183 (≠ S277) modified: Disulfide link with 162
- C344 (≠ A432) modified: Disulfide link with 370
- C370 (≠ A458) modified: Disulfide link with 344
- Y412 (= Y496) modified: 2',4',5'-topaquinone
- H467 (= H554) binding
- H469 (= H556) binding
- D476 (= D563) binding
- F477 (≠ L564) binding
- D478 (= D565) binding
- D617 (= D708) binding
- I618 (≠ A709) binding
- H628 (= H719) binding
8j6gA Neutron structure of copper amine oxidase from arthrobacter globiformis anaerobically reduced by phenylethylamine at pd 9.0
29% identity, 83% coverage: 125:750/757 of query aligns to 4:616/621 of 8j6gA
5zpnA Copper amine oxidase from arthrobacter globiformis anaerobically reduced by phenylethylamine at ph 8 at 288 k (1) (see paper)
29% identity, 83% coverage: 125:750/757 of query aligns to 3:615/620 of 5zpnA
- active site: Y276 (= Y399), D290 (= D413), Y374 (= Y496), H423 (= H554), H425 (= H556), H584 (= H719)
- binding copper (ii) ion: H423 (= H554), H425 (= H556), H584 (= H719)
- binding phenylacetaldehyde: L129 (= L255), Y288 (= Y411), D290 (= D413), Y294 (= Y417), I371 (≠ V493), G372 (= G494), Y374 (= Y496)
3x3xA Copper amine oxidase from arthrobacter globiformis anaerobically reduced by phenylethylamine (see paper)
29% identity, 83% coverage: 125:750/757 of query aligns to 3:615/620 of 3x3xA
- active site: Y276 (= Y399), D290 (= D413), Y374 (= Y496), H423 (= H554), H425 (= H556), H584 (= H719)
- binding copper (ii) ion: H423 (= H554), H425 (= H556), H584 (= H719)
- binding glycerol: I31 (≠ F153), Y33 (≠ E155), V243 (≠ S366), S321 (≠ A444), D322 (= D445), R362 (≠ E484), E389 (≠ G511), E391 (≠ D513)
- binding 2-phenyl-ethanol: P128 (= P254), L129 (= L255), Y288 (= Y411), D290 (= D413), Y294 (= Y417), I371 (≠ V493), G372 (= G494), N373 (= N495)
2cg1A Agao in complex with wc11b (ru-wire inhibitor, 11-carbon linker, data set b) (see paper)
29% identity, 83% coverage: 125:750/757 of query aligns to 3:615/620 of 2cg1A
- active site: Y276 (= Y399), D290 (= D413), Y374 (= Y496), H423 (= H554), H425 (= H556), H584 (= H719)
- binding ruthenium wire, 11 carbon linker: F97 (= F222), P128 (= P254), L129 (= L255), Y288 (= Y411), Y294 (= Y417), Y299 (≠ L422), T370 (= T492), G372 (= G494), Y374 (= Y496)
- binding copper (ii) ion: H423 (= H554), H425 (= H556), H584 (= H719)
2cg0A Agao in complex with wc9a (ru-wire inhibitor, 9-carbon linker, data set a) (see paper)
29% identity, 83% coverage: 125:750/757 of query aligns to 3:615/620 of 2cg0A
- active site: Y276 (= Y399), D290 (= D413), Y374 (= Y496), H423 (= H554), H425 (= H556), H584 (= H719)
- binding copper (ii) ion: H423 (= H554), H425 (= H556), H584 (= H719)
- binding ruthenium wire, 9 carbon linker: F97 (= F222), L129 (= L255), Y288 (= Y411), Y294 (= Y417), Y299 (≠ L422), G372 (= G494), Y374 (= Y496)
2cfwA Agao in complex with wc7a (ru-wire inhibitor, 7-carbon linker, data set a) (see paper)
29% identity, 83% coverage: 125:750/757 of query aligns to 3:615/620 of 2cfwA
- active site: Y276 (= Y399), D290 (= D413), Y374 (= Y496), H423 (= H554), H425 (= H556), H584 (= H719)
- binding copper (ii) ion: H423 (= H554), H425 (= H556), H584 (= H719)
- binding ruthenium wire, 7 carbon linker: F97 (= F222), P128 (= P254), L129 (= L255), Y288 (= Y411), Y294 (= Y417), Y299 (≠ L422), A300 (≠ T423), G372 (= G494), Y374 (= Y496)
2cflA Agao in complex with wc6b (ru-wire inhibitor, 6-carbon linker, data set b) (see paper)
29% identity, 83% coverage: 125:750/757 of query aligns to 3:615/620 of 2cflA
- active site: Y276 (= Y399), D290 (= D413), Y374 (= Y496), H423 (= H554), H425 (= H556), H584 (= H719)
- binding copper (ii) ion: H423 (= H554), H425 (= H556), H584 (= H719)
- binding ruthenium wire, 6 carbon linker: E94 (≠ L219), F97 (= F222), L129 (= L255), Y288 (= Y411), Y294 (= Y417), G372 (= G494), Y374 (= Y496)
2cfkA Agao in complex with wc5 (ru-wire inhibitor, 5-carbon linker) (see paper)
29% identity, 83% coverage: 125:750/757 of query aligns to 3:615/620 of 2cfkA
- active site: Y276 (= Y399), D290 (= D413), Y374 (= Y496), H423 (= H554), H425 (= H556), H584 (= H719)
- binding copper (ii) ion: H423 (= H554), H425 (= H556), H584 (= H719)
- binding ruthenium wire, 5 carbon linker: E94 (≠ L219), F97 (= F222), P128 (= P254), L129 (= L255), Y288 (= Y411), Y294 (= Y417), Y299 (≠ L422), T370 (= T492), G372 (= G494), Y374 (= Y496)
- binding ruthenium wire wc5: E94 (≠ L219), F97 (= F222), E98 (≠ A223), P128 (= P254), L129 (= L255), Y288 (= Y411), Y294 (= Y417), R328 (≠ M451), G372 (= G494), Y374 (= Y496)
2bt3A Agao in complex with ruthenium-c4-wire at 1.73 angstroms (see paper)
29% identity, 83% coverage: 125:750/757 of query aligns to 3:615/620 of 2bt3A
- active site: Y276 (= Y399), D290 (= D413), Y374 (= Y496), H423 (= H554), H425 (= H556), H584 (= H719)
- binding copper (ii) ion: H423 (= H554), H425 (= H556), H584 (= H719)
- 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 (≠ L219), F97 (= F222), P128 (= P254), L129 (= L255), Y288 (= Y411), Y294 (= Y417), Q298 (≠ T421), Y299 (≠ L422), R328 (≠ M451), G372 (= G494), Y374 (= Y496)
1rjoA Agao + xe (see paper)
29% identity, 83% coverage: 125:750/757 of query aligns to 3:615/620 of 1rjoA
- active site: Y276 (= Y399), D290 (= D413), Y374 (= Y496), H423 (= H554), H425 (= H556), H584 (= H719)
- binding copper (ii) ion: H423 (= H554), H425 (= H556), H584 (= H719)
- binding xenon: I12 (= I134), V15 (≠ A137), Q16 (≠ V138), I31 (≠ F153), L34 (≠ I156), R63 (≠ H191), L82 (≠ I210), D83 (≠ K211), I230 (= I353), W232 (= W355), W235 (= W358), L237 (≠ F360), G325 (= G448), M363 (≠ L485), I365 (≠ V487), W380 (= W502), Y381 (≠ I503), L382 (≠ F504), A392 (= A514), A394 (= A516), F427 (≠ Y558), L582 (≠ T717)
Query Sequence
>15508 FitnessBrowser__Keio:15508
MGSPSLYSARKTTLALAVALSFAWQAPVFAHGGEAHMVPMDKTLKEFGADVQWDDYAQLF
TLIKDGAYVKVKPGAQTAIVNGQPLALQVPVVMKDNKAWVSDTFINDVFQSGLDQTFQVE
KRPHPLNALTADEIKQAVEIVKASADFKPNTRFTEISLLPPDKEAVWAFALENKPVDQPR
KADVIMLDGKHIIEAVVDLQNNKLLSWQPIKDAHGMVLLDDFASVQNIINNSEEFAAAVK
KRGITDAKKVITTPLTVGYFDGKDGLKQDARLLKVISYLDVGDGNYWAHPIENLVAVVDL
EQKKIVKIEEGPVVPVPMTARPFDGRDRVAPAVKPMQIIEPEGKNYTITGDMIHWRNWDF
HLSMNSRVGPMISTVTYNDNGTKRKVMYEGSLGGMIVPYGDPDIGWYFKAYLDSGDYGMG
TLTSPIARGKDAPSNAVLLNETIADYTGVPMEIPRAIAVFERYAGPEYKHQEMGQPNVST
ERRELVVRWISTVGNYDYIFDWIFHENGTIGIDAGATGIEAVKGVKAKTMHDETAKDDTR
YGTLIDHNIVGTTHQHIYNFRLDLDVDGENNSLVAMDPVVKPNTAGGPRTSTMQVNQYNI
GNEQDAAQKFDPGTIRLLSNPNKENRMGNPVSYQIIPYAGGTHPVAKGAQFAPDEWIYHR
LSFMDKQLWVTRYHPGERFPEGKYPNRSTHDTGLGQYSKDNESLDNTDAVVWMTTGTTHV
ARAEEWPIMPTEWVHTLLKPWNFFDETPTLGALKKDK
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