SitesBLAST
Comparing 1936924 FitnessBrowser__Keio:1936924 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)
P06864 Evolved beta-galactosidase subunit alpha; Beta-gal; Lactase; EC 3.2.1.23 from Escherichia coli (strain K12) (see paper)
100% identity, 100% coverage: 1:1030/1030 of query aligns to 1:1030/1030 of P06864
- E449 (= E449) active site, Proton donor
6s6zA Structure of beta-galactosidase from thermotoga maritima (see paper)
37% identity, 97% coverage: 4:997/1030 of query aligns to 4:979/1083 of 6s6zA
3obaA Structure of the beta-galactosidase from kluyveromyces lactis (see paper)
35% identity, 96% coverage: 6:997/1030 of query aligns to 10:1021/1024 of 3obaA
- active site: D186 (= D190), H354 (= H342), H388 (= H376), E413 (= E401), H415 (= H403), E481 (= E449), Y522 (= Y490), E550 (= E512), H615 (≠ N572), F619 (= F576), D622 (= D579)
- binding manganese (iii) ion: D592 (vs. gap), H974 (= H950), D977 (≠ E953)
3ob8A Structure of the beta-galactosidase from kluyveromyces lactis in complex with galactose (see paper)
35% identity, 96% coverage: 6:997/1030 of query aligns to 10:1021/1024 of 3ob8A
- active site: D186 (= D190), H354 (= H342), H388 (= H376), E413 (= E401), H415 (= H403), E481 (= E449), Y522 (= Y490), E550 (= E512), H615 (≠ N572), F619 (= F576), D622 (= D579)
- binding beta-D-galactopyranose: D186 (= D190), H388 (= H376), N480 (= N448), E481 (= E449), M521 (= M489), E550 (= E512), H553 (= H515), W581 (= W543)
- binding magnesium ion: E413 (= E401), H415 (= H403), E481 (= E449)
- binding manganese (ii) ion: D592 (vs. gap), H974 (= H950), D977 (≠ E953)
1jz6A E. Coli (lacz) beta-galactosidase in complex with galacto-tetrazole (see paper)
34% identity, 95% coverage: 4:980/1030 of query aligns to 4:991/1011 of 1jz6A
- active site: D189 (= D190), H345 (= H342), H379 (= H376), E404 (= E401), H406 (= H403), E449 (= E449), Y491 (= Y490), E525 (= E512), N585 (= N572), F589 (= F576), N592 (≠ D579)
- binding (5r, 6s, 7s, 8s)-5-hydroxymethyl-6,7,8-trihydroxy-tetrazolo[1,5-a]piperidine: D189 (= D190), H379 (= H376), E449 (= E449), Y491 (= Y490), E525 (= E512), H528 (= H515), W556 (= W543), N592 (≠ D579)
- binding magnesium ion: N6 (= N6), V9 (≠ L9), Q151 (≠ K152), D181 (= D182), E404 (= E401), H406 (= H403), E449 (= E449), S635 (≠ L625), E638 (≠ Y628), L658 (= L648)
- binding sodium ion: D189 (= D190), F544 (= F531), Y547 (≠ H534), P548 (≠ D535), L550 (≠ I537), F589 (= F576), C590 (= C577), N592 (≠ D579), F919 (= F902), P920 (= P903), L955 (≠ I945), M956 (≠ H946), T958 (≠ A948)
Sites not aligning to the query:
1jz5A E. Coli (lacz) beta-galactosidase in complex with d-galctopyranosyl-1- on (see paper)
34% identity, 95% coverage: 4:980/1030 of query aligns to 4:991/1011 of 1jz5A
- active site: D189 (= D190), H345 (= H342), H379 (= H376), E404 (= E401), H406 (= H403), E449 (= E449), Y491 (= Y490), E525 (= E512), N585 (= N572), F589 (= F576), N592 (≠ D579)
- binding D-galactonolactone: D189 (= D190), H379 (= H376), N448 (= N448), E449 (= E449), M490 (= M489), Y491 (= Y490), E525 (= E512), H528 (= H515), W556 (= W543), F589 (= F576), N592 (≠ D579)
- binding magnesium ion: N6 (= N6), V9 (≠ L9), Q151 (≠ K152), D181 (= D182), E404 (= E401), H406 (= H403), E449 (= E449)
Sites not aligning to the query:
1jz3A E. Coli (lacz) beta-galactosidase-trapped 2-deoxy-galactosyl enzyme intermediate (see paper)
34% identity, 95% coverage: 4:980/1030 of query aligns to 4:991/1011 of 1jz3A
- active site: D189 (= D190), H345 (= H342), H379 (= H376), E404 (= E401), H406 (= H403), E449 (= E449), Y491 (= Y490), E525 (= E512), N585 (= N572), F589 (= F576), N592 (≠ D579)
- binding 2-deoxy-alpha-D-galactopyranose: D189 (= D190), H379 (= H376), E449 (= E449), Y491 (= Y490), E525 (= E512), H528 (= H515), W556 (= W543), F589 (= F576)
- binding magnesium ion: N6 (= N6), V9 (≠ L9), Q151 (≠ K152), D181 (= D182), E404 (= E401), H406 (= H403), E449 (= E449)
Sites not aligning to the query:
1jz2A E. Coli (lacz) beta-galactosidase-trapped 2-f-galactosyl-enzyme intermediate (orthorhombic) (see paper)
34% identity, 95% coverage: 4:980/1030 of query aligns to 4:991/1011 of 1jz2A
- active site: D189 (= D190), H345 (= H342), H379 (= H376), E404 (= E401), H406 (= H403), E449 (= E449), Y491 (= Y490), E525 (= E512), N585 (= N572), F589 (= F576), N592 (≠ D579)
- binding 2-deoxy-2-fluoro-beta-D-galactopyranose: D189 (= D190), H379 (= H376), N448 (= N448), E449 (= E449), Y491 (= Y490), E525 (= E512), H528 (= H515), W556 (= W543), F589 (= F576)
- binding magnesium ion: N6 (= N6), V9 (≠ L9), Q151 (≠ K152), D181 (= D182), E404 (= E401), H406 (= H403), E449 (= E449)
- binding sodium ion: D189 (= D190), F544 (= F531), Y547 (≠ H534), P548 (≠ D535), L550 (≠ I537), Q551 (= Q538), F589 (= F576), N592 (≠ D579), F919 (= F902), P920 (= P903), L955 (≠ I945), M956 (≠ H946), T958 (≠ A948)
Sites not aligning to the query:
1jyxA E. Coli (lacz) beta-galactosidase in complex with iptg (see paper)
34% identity, 95% coverage: 4:980/1030 of query aligns to 4:991/1011 of 1jyxA
- active site: D189 (= D190), H345 (= H342), H379 (= H376), E404 (= E401), H406 (= H403), E449 (= E449), Y491 (= Y490), E525 (= E512), N585 (= N572), F589 (= F576), N592 (≠ D579)
- binding 1-methylethyl 1-thio-beta-D-galactopyranoside: N90 (≠ D92), D189 (= D190), E292 (= E289), P294 (= P291), E449 (= E449), E525 (= E512), H528 (= H515), N592 (≠ D579), R633 (≠ T623), D636 (= D626), Q690 (≠ K679), W696 (≠ Y685), W987 (= W976)
- binding magnesium ion: N6 (= N6), V9 (≠ L9), Q151 (≠ K152), D181 (= D182), E404 (= E401), H406 (= H403), E449 (= E449)
- binding sodium ion: D189 (= D190), F544 (= F531), Y547 (≠ H534), P548 (≠ D535), L550 (≠ I537), Q551 (= Q538), F589 (= F576), C590 (= C577), N592 (≠ D579), F919 (= F902), P920 (= P903), L955 (≠ I945), M956 (≠ H946), T958 (≠ A948)
Sites not aligning to the query:
6tshA Beta-galactosidase in complex with deoxygalacto-nojirimycin (see paper)
34% identity, 95% coverage: 4:980/1030 of query aligns to 8:995/1015 of 6tshA
- binding (2R,3S,4R,5S)-2-(hydroxymethyl)piperidine-3,4,5-triol: D193 (= D190), H383 (= H376), E453 (= E449), E529 (= E512), H532 (= H515), W560 (= W543), F593 (= F576)
- binding magnesium ion: E408 (= E401), H410 (= H403), E453 (= E449)
5a1aA 2.2 a resolution cryo-em structure of beta-galactosidase in complex with a cell-permeant inhibitor (see paper)
34% identity, 95% coverage: 4:980/1030 of query aligns to 15:1002/1022 of 5a1aA
- active site: D200 (= D190), H356 (= H342), H390 (= H376), E415 (= E401), H417 (= H403), E460 (= E449), Y502 (= Y490), E536 (= E512), N596 (= N572), F600 (= F576), N603 (≠ D579)
- binding magnesium ion: W15 (= W4), N17 (= N6), V20 (≠ L9), Q162 (≠ K152), D192 (= D182), E415 (= E401), H417 (= H403), E460 (= E449)
- binding sodium ion: D200 (= D190), H539 (= H515), F555 (= F531), Y558 (≠ H534), P559 (≠ D535), L561 (≠ I537), F600 (= F576), N603 (≠ D579)
- binding 2-phenylethyl 1-thio-beta-D-galactopyranoside: N101 (≠ D92), D200 (= D190), M501 (= M489), Y502 (= Y490), H539 (= H515), D597 (≠ N573), F600 (= F576), W998 (= W976)
Sites not aligning to the query:
P00722 Beta-galactosidase; Beta-gal; Lactase; EC 3.2.1.23 from Escherichia coli (strain K12) (see 13 papers)
34% identity, 95% coverage: 4:980/1030 of query aligns to 17:1004/1024 of P00722
- D202 (= D190) mutation D->E,N: Causes a significant decrease in binding affinity in the absence of monovalent cations or in the presence of potassium ions, but only a moderate decrease in the presence of sodium ions.; mutation to F: Obliterates all binding and catalysis.
- H358 (= H342) mutation H->D,F,L,N: Less stable to heat than wild-type. Causes significant destabilizations of the first transition state.
- H392 (= H376) mutation H->E,F,K: Essentially inactive unless very rapid purification. Causes very large destabilizations of the transition state.
- E417 (= E401) binding
- H419 (= H403) binding
- E462 (= E449) active site, Proton donor; binding ; mutation to H: Slowly inactivates galactosidase activity by reducing the binding of magnesium. It increases binding specificity.
- E538 (= E512) active site, Nucleophile; mutation to Q: 10000-fold decrease in the beta-galactosidase activity.
- H541 (= H515) mutation H->E,F,N: Poorly reactive with galactosyl substrates. Less stable to heat than wild-type.
- N598 (= N572) binding
- F602 (= F576) mutation to A: Decreases the stability of the loop 794-804.
- G795 (≠ Q773) mutation to A: It forces the apoenzyme to adopt the closed rather than the open conformation. Reduces the binding affinity.
- E798 (= E776) mutation E->A,L: The catalytic efficiency is not increased, when the sodium concentration increases.; mutation E->D,Q: Small increase of the catalytic efficiency, when the sodium concentration increases.
- W1000 (= W976) mutation W->F,G,L,T: Decreases affinity for substrate.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
7brsA E.Coli beta-galactosidase (e537q) in complex with fluorescent probe ksa02 (see paper)
34% identity, 95% coverage: 4:980/1030 of query aligns to 14:1001/1021 of 7brsA
- binding 8-[2-[(E)-2-[4-[(2S,3R,4S,5R,6R)-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxyphenyl]ethenyl]-3,3-dimethyl-indol-1-ium-1-yl]octanoic acid: N100 (≠ D92), D199 (= D190), E459 (= E449), Y501 (= Y490), Q535 (≠ E512), H538 (= H515), N602 (≠ D579), W997 (= W976)
- binding magnesium ion: N16 (= N6), V19 (≠ L9), Q161 (≠ K152), D191 (= D182), E414 (= E401), H416 (= H403), E459 (= E449)
Sites not aligning to the query:
6kuzA E.Coli beta-galactosidase (e537q) in complex with fluorescent probe ksl01 (see paper)
34% identity, 95% coverage: 4:980/1030 of query aligns to 14:1001/1021 of 6kuzA
- binding 3-(1,3-benzothiazol-2-yl)-2-[[4-[(2~{S},3~{R},4~{S},5~{R},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxyphenyl]methoxy]-5-methyl-benzaldehyde: N100 (≠ D92), D199 (= D190), H389 (= H376), H416 (= H403), E459 (= E449), Y501 (= Y490), Q535 (≠ E512), H538 (= H515), W566 (= W543), W997 (= W976)
- binding magnesium ion: N16 (= N6), V19 (≠ L9), Q161 (≠ K152), D191 (= D182), E414 (= E401), H416 (= H403), E459 (= E449)
Sites not aligning to the query:
1jywA E. Coli (lacz) beta-galactosidase (e537q) in complex with pnpg (see paper)
34% identity, 95% coverage: 4:980/1030 of query aligns to 4:991/1011 of 1jywA
- active site: D189 (= D190), H345 (= H342), H379 (= H376), E404 (= E401), H406 (= H403), E449 (= E449), Y491 (= Y490), Q525 (≠ E512), N585 (= N572), F589 (= F576), N592 (≠ D579)
- binding 4-nitrophenyl beta-D-galactopyranoside: N90 (≠ D92), D189 (= D190), E449 (= E449), Y491 (= Y490), Q525 (≠ E512), H528 (= H515), N592 (≠ D579), W987 (= W976)
- binding magnesium ion: N6 (= N6), V9 (≠ L9), Q151 (≠ K152), D181 (= D182), E404 (= E401), H406 (= H403), E449 (= E449)
Sites not aligning to the query:
1jyvA E. Coli (lacz) beta-galactosidase (e537q) in complex with onpg (see paper)
34% identity, 95% coverage: 4:980/1030 of query aligns to 4:991/1011 of 1jyvA
- active site: D189 (= D190), H345 (= H342), H379 (= H376), E404 (= E401), H406 (= H403), E449 (= E449), Y491 (= Y490), Q525 (≠ E512), N585 (= N572), F589 (= F576), N592 (≠ D579)
- binding 2-nitrophenyl beta-D-galactopyranoside: N90 (≠ D92), N90 (≠ D92), V91 (≠ E93), D189 (= D190), H406 (= H403), E449 (= E449), Y491 (= Y490), H528 (= H515), D586 (≠ N573), F589 (= F576), N592 (≠ D579), V783 (≠ E774), V783 (≠ E774), E785 (= E776), R788 (vs. gap), W987 (= W976)
- binding magnesium ion: N6 (= N6), V9 (≠ L9), Q151 (≠ K152), D181 (= D182), E404 (= E401), H406 (= H403), E449 (= E449)
Sites not aligning to the query:
1jynA E. Coli (lacz) beta-galactosidase (e537q) in complex with lactose (see paper)
34% identity, 95% coverage: 4:980/1030 of query aligns to 4:991/1011 of 1jynA
- active site: D189 (= D190), H345 (= H342), H379 (= H376), E404 (= E401), H406 (= H403), E449 (= E449), Y491 (= Y490), Q525 (≠ E512), N585 (= N572), F589 (= F576), N592 (≠ D579)
- binding beta-D-glucopyranose: N90 (≠ D92), W987 (= W976)
- binding beta-D-galactopyranose: N90 (≠ D92), D189 (= D190), E449 (= E449), Y491 (= Y490), H528 (= H515), N592 (≠ D579), W987 (= W976)
- binding magnesium ion: N6 (= N6), V9 (≠ L9), Q151 (≠ K152), D181 (= D182), E404 (= E401), H406 (= H403), E449 (= E449)
- binding sodium ion: D189 (= D190), F544 (= F531), Y547 (≠ H534), P548 (≠ D535), L550 (≠ I537), F589 (= F576), N592 (≠ D579), S635 (≠ L625), D636 (= D626), E638 (≠ Y628), L658 (= L648), F919 (= F902), P920 (= P903), L955 (≠ I945), M956 (≠ H946), T958 (≠ A948)
Sites not aligning to the query:
7btkC E.Coli beta-galactosidase (e537q) in complex with fluorescent probe ksa01 (see paper)
34% identity, 95% coverage: 4:980/1030 of query aligns to 16:1003/1023 of 7btkC
- binding 4-[[2-[(E)-2-[4-[(2S,3R,4S,5R,6R)-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxyphenyl]ethenyl]-3,3-dimethyl-2H-indol-1-yl]methyl]benzoic acid: N102 (≠ D92), D201 (= D190), H391 (= H376), N460 (= N448), E461 (= E449), Y503 (= Y490), F512 (= F499), Q537 (≠ E512), W568 (= W543), W999 (= W976)
- binding magnesium ion: N18 (= N6), V21 (≠ L9), Q163 (≠ K152), D193 (= D182), D201 (= D190), E416 (= E401), H418 (= H403), E461 (= E449)
Sites not aligning to the query:
4duxA E. Coli (lacz) beta-galactosidase (n460s) in complex with l-ribose (see paper)
34% identity, 95% coverage: 4:980/1030 of query aligns to 8:995/1015 of 4duxA
- active site: D193 (= D190), H349 (= H342), H383 (= H376), E408 (= E401), H410 (= H403), E453 (= E449), Y495 (= Y490), E529 (= E512), N589 (= N572), F593 (= F576), N596 (≠ D579)
- binding beta-L-ribopyranose: D193 (= D190), H383 (= H376), E453 (= E449), M494 (= M489), Y495 (= Y490), E529 (= E512), H532 (= H515), W560 (= W543), F593 (= F576), S788 (≠ Y775), W991 (= W976)
- binding magnesium ion: N10 (= N6), V13 (≠ L9), Q155 (≠ K152), D185 (= D182), E408 (= E401), H410 (= H403), E453 (= E449)
Sites not aligning to the query:
3bgaA Crystal structure of beta-galactosidase from bacteroides thetaiotaomicron vpi-5482
32% identity, 97% coverage: 4:1003/1030 of query aligns to 4:998/1003 of 3bgaA
- active site: D201 (= D190), H354 (= H342), H387 (= H376), E412 (= E401), H414 (= H403), E458 (= E449), Y499 (= Y490), E522 (= E512), S584 (≠ N572), F588 (= F576), N591 (≠ D579)
- binding magnesium ion: E412 (= E401), H414 (= H403), E458 (= E449)
Query Sequence
>1936924 FitnessBrowser__Keio:1936924
MNRWENIQLTHENRLAPRAYFFSYDSVAQARTFARETSSLFLPLSGQWNFHFFDHPLQVP
EAFTSELMADWGHITVPAMWQMEGHGKLQYTDEGFPFPIDVPFVPSDNPTGAYQRIFTLS
DGWQGKQTLIKFDGVETYFEVYVNGQYVGFSKGSRLTAEFDISAMVKTGDNLLCVRVMQW
ADSTYVEDQDMWWSAGIFRDVYLVGKHLTHINDFTVRTDFDEAYCDATLSCEVVLENLAA
SPVVTTLEYTLFDGERVVHSSAIDHLAIEKLTSASFAFTVEQPQQWSAESPYLYHLVMTL
KDANGNVLEVVPQRVGFRDIKVRDGLFWINNRYVMLHGVNRHDNDHRKGRAVGMDRVEKD
LQLMKQHNINSVRTAHYPNDPRFYELCDIYGLFVMAETDVESHGFANVGDISRITDDPQW
EKVYVERIVRHIHAQKNHPSIIIWSLGNESGYGCNIRAMYHAAKALDDTRLVHYEEDRDA
EVVDIISTMYTRVPLMNEFGEYPHPKPRIICEYAHAMGNGPGGLTEYQNVFYKHDCIQGH
YVWEWCDHGIQAQDDHGNVWYKFGGDYGDYPNNYNFCLDGLIYSDQTPGPGLKEYKQVIA
PVKIHARDLTRGELKVENKLWFTTLDDYTLHAEVRAEGETLATQQIKLRDVAPNSEAPLQ
ITLPQLDAREAFLNITVTKDSRTRYSEAGHPIATYQFPLKENTAQPVPFAPNNARPLTLE
DDRLSCTVRGYNFAITFSKMSGKPTSWQVNGESLLTREPKINFFKPMIDNHKQEYEGLWQ
PNHLQIMQEHLRDFAVEQSDGEVLIISRTVIAPPVFDFGMRCTYIWRIAADGQVNVALSG
ERYGDYPHIIPCIGFTMGINGEYDQVAYYGRGPGENYADSQQANIIDIWRSTVDAMFENY
PFPQNNGNRQHVRWTALTNRHGNGLLVVPQRPINFSAWHYTQENIHAAQHCNELQRSDDI
TLNLDHQLLGLGSNSWGSEVLDSWRVWFRDFSYGFTLLPVSGGEATAQSLASYEFGAGFF
STNLHSENKQ
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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