SitesBLAST
Comparing 352867 FitnessBrowser__Btheta:352867 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)
6s6zA Structure of beta-galactosidase from thermotoga maritima (see paper)
39% identity, 97% coverage: 26:1028/1036 of query aligns to 3:979/1083 of 6s6zA
3bgaA Crystal structure of beta-galactosidase from bacteroides thetaiotaomicron vpi-5482
39% identity, 97% coverage: 26:1031/1036 of query aligns to 3:995/1003 of 3bgaA
- active site: D201 (= D220), H354 (= H361), H387 (= H395), E412 (= E420), H414 (= H422), E458 (= E466), Y499 (= Y507), E522 (= E529), S584 (= S590), F588 (= F594), N591 (= N597)
- binding magnesium ion: E412 (= E420), H414 (= H422), E458 (= E466)
1jz6A E. Coli (lacz) beta-galactosidase in complex with galacto-tetrazole (see paper)
34% identity, 97% coverage: 26:1027/1036 of query aligns to 3:1007/1011 of 1jz6A
- active site: D189 (= D220), H345 (= H361), H379 (= H395), E404 (= E420), H406 (= H422), E449 (= E466), Y491 (= Y507), E525 (= E529), N585 (≠ S590), F589 (= F594), N592 (= N597)
- binding (5r, 6s, 7s, 8s)-5-hydroxymethyl-6,7,8-trihydroxy-tetrazolo[1,5-a]piperidine: D189 (= D220), H379 (= H395), E449 (= E466), Y491 (= Y507), E525 (= E529), H528 (= H532), W556 (= W560), N592 (= N597)
- binding magnesium ion: D3 (≠ E26), N6 (≠ D29), V9 (= V32), Q151 (≠ E182), D181 (= D212), E404 (= E420), H406 (= H422), E449 (= E466), S635 (≠ L643), E638 (≠ F646), L658 (= L667)
- binding sodium ion: D189 (= D220), F544 (≠ T548), Y547 (= Y551), P548 (= P552), L550 (≠ Y554), F589 (= F594), C590 (≠ N595), N592 (= N597), F919 (≠ R927), P920 (= P928), L955 (= L970), M956 (≠ D971), T958 (≠ G973)
1jz5A E. Coli (lacz) beta-galactosidase in complex with d-galctopyranosyl-1- on (see paper)
34% identity, 97% coverage: 26:1027/1036 of query aligns to 3:1007/1011 of 1jz5A
- active site: D189 (= D220), H345 (= H361), H379 (= H395), E404 (= E420), H406 (= H422), E449 (= E466), Y491 (= Y507), E525 (= E529), N585 (≠ S590), F589 (= F594), N592 (= N597)
- binding D-galactonolactone: D189 (= D220), H379 (= H395), N448 (= N465), E449 (= E466), M490 (= M506), Y491 (= Y507), E525 (= E529), H528 (= H532), W556 (= W560), F589 (= F594), N592 (= N597)
- binding magnesium ion: D3 (≠ E26), N6 (≠ D29), V9 (= V32), Q151 (≠ E182), D181 (= D212), E404 (= E420), H406 (= H422), E449 (= E466)
1jz3A E. Coli (lacz) beta-galactosidase-trapped 2-deoxy-galactosyl enzyme intermediate (see paper)
34% identity, 97% coverage: 26:1027/1036 of query aligns to 3:1007/1011 of 1jz3A
- active site: D189 (= D220), H345 (= H361), H379 (= H395), E404 (= E420), H406 (= H422), E449 (= E466), Y491 (= Y507), E525 (= E529), N585 (≠ S590), F589 (= F594), N592 (= N597)
- binding 2-deoxy-alpha-D-galactopyranose: D189 (= D220), H379 (= H395), E449 (= E466), Y491 (= Y507), E525 (= E529), H528 (= H532), W556 (= W560), F589 (= F594)
- binding magnesium ion: D3 (≠ E26), N6 (≠ D29), V9 (= V32), Q151 (≠ E182), D181 (= D212), E404 (= E420), H406 (= H422), E449 (= E466)
1jz2A E. Coli (lacz) beta-galactosidase-trapped 2-f-galactosyl-enzyme intermediate (orthorhombic) (see paper)
34% identity, 97% coverage: 26:1027/1036 of query aligns to 3:1007/1011 of 1jz2A
- active site: D189 (= D220), H345 (= H361), H379 (= H395), E404 (= E420), H406 (= H422), E449 (= E466), Y491 (= Y507), E525 (= E529), N585 (≠ S590), F589 (= F594), N592 (= N597)
- binding 2-deoxy-2-fluoro-beta-D-galactopyranose: D189 (= D220), H379 (= H395), N448 (= N465), E449 (= E466), Y491 (= Y507), E525 (= E529), H528 (= H532), W556 (= W560), F589 (= F594)
- binding magnesium ion: D3 (≠ E26), N6 (≠ D29), V9 (= V32), Q151 (≠ E182), D181 (= D212), E404 (= E420), H406 (= H422), E449 (= E466)
- binding sodium ion: D189 (= D220), F544 (≠ T548), Y547 (= Y551), P548 (= P552), L550 (≠ Y554), Q551 (= Q555), F589 (= F594), N592 (= N597), F919 (≠ R927), P920 (= P928), L955 (= L970), M956 (≠ D971), T958 (≠ G973)
1jyxA E. Coli (lacz) beta-galactosidase in complex with iptg (see paper)
34% identity, 97% coverage: 26:1027/1036 of query aligns to 3:1007/1011 of 1jyxA
- active site: D189 (= D220), H345 (= H361), H379 (= H395), E404 (= E420), H406 (= H422), E449 (= E466), Y491 (= Y507), E525 (= E529), N585 (≠ S590), F589 (= F594), N592 (= N597)
- binding 1-methylethyl 1-thio-beta-D-galactopyranoside: N90 (= N117), D189 (= D220), E292 (= E309), P294 (= P311), E449 (= E466), E525 (= E529), H528 (= H532), N592 (= N597), R633 (= R641), D636 (≠ S644), Q690 (≠ L700), W696 (≠ L706), W987 (= W1007)
- binding magnesium ion: D3 (≠ E26), N6 (≠ D29), V9 (= V32), Q151 (≠ E182), D181 (= D212), E404 (= E420), H406 (= H422), E449 (= E466)
- binding sodium ion: D189 (= D220), F544 (≠ T548), Y547 (= Y551), P548 (= P552), L550 (≠ Y554), Q551 (= Q555), F589 (= F594), C590 (≠ N595), N592 (= N597), F919 (≠ R927), P920 (= P928), L955 (= L970), M956 (≠ D971), T958 (≠ G973)
P00722 Beta-galactosidase; Beta-gal; Lactase; EC 3.2.1.23 from Escherichia coli (strain K12) (see 13 papers)
34% identity, 97% coverage: 26:1027/1036 of query aligns to 16:1020/1024 of P00722
- D202 (= D220) 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 (= H361) mutation H->D,F,L,N: Less stable to heat than wild-type. Causes significant destabilizations of the first transition state.
- H392 (= H395) mutation H->E,F,K: Essentially inactive unless very rapid purification. Causes very large destabilizations of the transition state.
- E417 (= E420) binding
- H419 (= H422) binding
- E462 (= E466) active site, Proton donor; binding ; mutation to H: Slowly inactivates galactosidase activity by reducing the binding of magnesium. It increases binding specificity.
- E538 (= E529) active site, Nucleophile; mutation to Q: 10000-fold decrease in the beta-galactosidase activity.
- H541 (= H532) mutation H->E,F,N: Poorly reactive with galactosyl substrates. Less stable to heat than wild-type.
- N598 (≠ S590) binding
- F602 (= F594) mutation to A: Decreases the stability of the loop 794-804.
- G795 (= G802) mutation to A: It forces the apoenzyme to adopt the closed rather than the open conformation. Reduces the binding affinity.
- E798 (≠ L805) 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 (= W1007) mutation W->F,G,L,T: Decreases affinity for substrate.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
6tshA Beta-galactosidase in complex with deoxygalacto-nojirimycin (see paper)
34% identity, 97% coverage: 26:1027/1036 of query aligns to 7:1011/1015 of 6tshA
- binding (2R,3S,4R,5S)-2-(hydroxymethyl)piperidine-3,4,5-triol: D193 (= D220), H383 (= H395), E453 (= E466), E529 (= E529), H532 (= H532), W560 (= W560), F593 (= F594)
- binding magnesium ion: E408 (= E420), H410 (= H422), E453 (= E466)
5a1aA 2.2 a resolution cryo-em structure of beta-galactosidase in complex with a cell-permeant inhibitor (see paper)
34% identity, 97% coverage: 26:1027/1036 of query aligns to 14:1018/1022 of 5a1aA
- active site: D200 (= D220), H356 (= H361), H390 (= H395), E415 (= E420), H417 (= H422), E460 (= E466), Y502 (= Y507), E536 (= E529), N596 (≠ S590), F600 (= F594), N603 (= N597)
- binding magnesium ion: D14 (≠ E26), W15 (= W27), N17 (≠ D29), V20 (= V32), Q162 (≠ E182), D192 (= D212), E415 (= E420), H417 (= H422), E460 (= E466)
- binding sodium ion: D200 (= D220), H539 (= H532), F555 (≠ T548), Y558 (= Y551), P559 (= P552), L561 (≠ Y554), F600 (= F594), N603 (= N597)
- binding 2-phenylethyl 1-thio-beta-D-galactopyranoside: N101 (= N117), D200 (= D220), M501 (= M506), Y502 (= Y507), H539 (= H532), D597 (= D591), F600 (= F594), W998 (= W1007)
P06864 Evolved beta-galactosidase subunit alpha; Beta-gal; Lactase; EC 3.2.1.23 from Escherichia coli (strain K12) (see paper)
32% identity, 97% coverage: 24:1031/1036 of query aligns to 1:1000/1030 of P06864
- E449 (= E466) active site, Proton donor
1jywA E. Coli (lacz) beta-galactosidase (e537q) in complex with pnpg (see paper)
34% identity, 97% coverage: 26:1027/1036 of query aligns to 3:1007/1011 of 1jywA
- active site: D189 (= D220), H345 (= H361), H379 (= H395), E404 (= E420), H406 (= H422), E449 (= E466), Y491 (= Y507), Q525 (≠ E529), N585 (≠ S590), F589 (= F594), N592 (= N597)
- binding 4-nitrophenyl beta-D-galactopyranoside: N90 (= N117), D189 (= D220), E449 (= E466), Y491 (= Y507), Q525 (≠ E529), H528 (= H532), N592 (= N597), W987 (= W1007)
- binding magnesium ion: D3 (≠ E26), N6 (≠ D29), V9 (= V32), Q151 (≠ E182), D181 (= D212), E404 (= E420), H406 (= H422), E449 (= E466)
1jyvA E. Coli (lacz) beta-galactosidase (e537q) in complex with onpg (see paper)
34% identity, 97% coverage: 26:1027/1036 of query aligns to 3:1007/1011 of 1jyvA
- active site: D189 (= D220), H345 (= H361), H379 (= H395), E404 (= E420), H406 (= H422), E449 (= E466), Y491 (= Y507), Q525 (≠ E529), N585 (≠ S590), F589 (= F594), N592 (= N597)
- binding 2-nitrophenyl beta-D-galactopyranoside: N90 (= N117), N90 (= N117), V91 (= V118), D189 (= D220), H406 (= H422), E449 (= E466), Y491 (= Y507), H528 (= H532), D586 (= D591), F589 (= F594), N592 (= N597), V783 (≠ A803), V783 (≠ A803), E785 (≠ L805), R788 (= R808), W987 (= W1007)
- binding magnesium ion: D3 (≠ E26), N6 (≠ D29), V9 (= V32), Q151 (≠ E182), D181 (= D212), E404 (= E420), H406 (= H422), E449 (= E466)
1jynA E. Coli (lacz) beta-galactosidase (e537q) in complex with lactose (see paper)
34% identity, 97% coverage: 26:1027/1036 of query aligns to 3:1007/1011 of 1jynA
- active site: D189 (= D220), H345 (= H361), H379 (= H395), E404 (= E420), H406 (= H422), E449 (= E466), Y491 (= Y507), Q525 (≠ E529), N585 (≠ S590), F589 (= F594), N592 (= N597)
- binding beta-D-glucopyranose: N90 (= N117), W987 (= W1007)
- binding beta-D-galactopyranose: N90 (= N117), D189 (= D220), E449 (= E466), Y491 (= Y507), H528 (= H532), N592 (= N597), W987 (= W1007)
- binding magnesium ion: D3 (≠ E26), N6 (≠ D29), V9 (= V32), Q151 (≠ E182), D181 (= D212), E404 (= E420), H406 (= H422), E449 (= E466)
- binding sodium ion: D189 (= D220), F544 (≠ T548), Y547 (= Y551), P548 (= P552), L550 (≠ Y554), F589 (= F594), N592 (= N597), S635 (≠ L643), D636 (≠ S644), E638 (≠ F646), L658 (= L667), F919 (≠ R927), P920 (= P928), L955 (= L970), M956 (≠ D971), T958 (≠ G973)
4duxA E. Coli (lacz) beta-galactosidase (n460s) in complex with l-ribose (see paper)
34% identity, 97% coverage: 26:1027/1036 of query aligns to 7:1011/1015 of 4duxA
- active site: D193 (= D220), H349 (= H361), H383 (= H395), E408 (= E420), H410 (= H422), E453 (= E466), Y495 (= Y507), E529 (= E529), N589 (≠ S590), F593 (= F594), N596 (= N597)
- binding beta-L-ribopyranose: D193 (= D220), H383 (= H395), E453 (= E466), M494 (= M506), Y495 (= Y507), E529 (= E529), H532 (= H532), W560 (= W560), F593 (= F594), S788 (≠ G804), W991 (= W1007)
- binding magnesium ion: D7 (≠ E26), N10 (≠ D29), V13 (= V32), Q155 (≠ E182), D185 (= D212), E408 (= E420), H410 (= H422), E453 (= E466)
7brsA E.Coli beta-galactosidase (e537q) in complex with fluorescent probe ksa02 (see paper)
34% identity, 97% coverage: 26:1027/1036 of query aligns to 13:1017/1021 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 (= N117), D199 (= D220), E459 (= E466), Y501 (= Y507), Q535 (≠ E529), H538 (= H532), N602 (= N597), W997 (= W1007)
- binding magnesium ion: D13 (≠ E26), N16 (≠ D29), V19 (= V32), Q161 (≠ E182), D191 (= D212), E414 (= E420), H416 (= H422), E459 (= E466)
6kuzA E.Coli beta-galactosidase (e537q) in complex with fluorescent probe ksl01 (see paper)
34% identity, 97% coverage: 26:1027/1036 of query aligns to 13:1017/1021 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 (= N117), D199 (= D220), H389 (= H395), H416 (= H422), E459 (= E466), Y501 (= Y507), Q535 (≠ E529), H538 (= H532), W566 (= W560), W997 (= W1007)
- binding magnesium ion: D13 (≠ E26), N16 (≠ D29), V19 (= V32), Q161 (≠ E182), D191 (= D212), E414 (= E420), H416 (= H422), E459 (= E466)
7btkC E.Coli beta-galactosidase (e537q) in complex with fluorescent probe ksa01 (see paper)
34% identity, 97% coverage: 26:1027/1036 of query aligns to 15:1019/1023 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 (= N117), D201 (= D220), H391 (= H395), N460 (= N465), E461 (= E466), Y503 (= Y507), F512 (≠ Y516), Q537 (≠ E529), W568 (= W560), W999 (= W1007)
- binding magnesium ion: D15 (≠ E26), N18 (≠ D29), V21 (= V32), Q163 (≠ E182), D193 (= D212), D201 (= D220), E416 (= E420), H418 (= H422), E461 (= E466)
1yq2A Beta-galactosidase from arthrobacter sp. C2-2 (isoenzyme c2-2-1) (see paper)
29% identity, 91% coverage: 65:1003/1036 of query aligns to 30:996/1020 of 1yq2A
- active site: D198 (= D220), H332 (= H361), H366 (= H395), E391 (= E420), H393 (= H422), E439 (= E466), Y480 (= Y507), E518 (= E529), H578 (≠ S590), F582 (= F594), D585 (≠ N597)
- binding magnesium ion: A522 (= A533), G524 (= G535), G526 (≠ S537)
6sebA Cold-adapted beta-d-galactosidase from arthrobacter sp. 32cb in complex with iptg (see paper)
29% identity, 93% coverage: 65:1029/1036 of query aligns to 37:986/989 of 6sebA
- binding 1-methylethyl 1-thio-beta-D-galactopyranoside: D186 (= D220), E420 (= E466), Y461 (= Y507), E496 (= E529), H499 (= H532), D887 (≠ F922), R939 (≠ S981), L942 (≠ V984), K943 (≠ E985), A944 (≠ K986), C964 (≠ W1007)
Query Sequence
>352867 FitnessBrowser__Btheta:352867
MKKQLLSCCLAALGLTTAIQAQNFNEWKDPEVNSVNRSAMHTNYFAYASADEAKAGSKED
SQNFMTLNGLWKFNWVRNADARPTNFYQTSFNDKGWDNIKVPAVWELNGYGDPIYVNVGY
AWRNQFQNNPPLVPTENNHVGSYRKEIVLPADWKGKDIFAHFGSVTSNMYLWVNGRYVGY
SEDSKLEAEFDLTNYLKPGKNLIAFQVFRWCDGSYLEDQDFFRYSGVGRDCYLYARDKKR
IQDIRVTPDLDSQYKDGTLNIAIDMKGSGTVALDLTDAQGKSVATADLKGSGKLNTTINV
ANPAKWTAETPNLYTLTATLKNGSTVTEVIPVKVGFRKIELTGGQILVNGQPVLFKGADR
HEMDPDGGYVVSLERMIQDIKVMKQLNINAVRTCHYPDDNRWYDLCDQYGLYVVAEANVE
SHGMGYGDKSLAKNPIYAKAHMERNQRNVQRGYNHPSIIFWSLGNEAGMGPNFEHCYTWI
KNEDKTRAVQYEQAGTSEFTDIFCPMYYDYNNCIKYCEGNIDKPLIQCEYAHAMGNSQGG
FKEYWDITRKYPKYQGGFIWDFVDQSCHWKNKDGVAIYGYGGDFNKYDASDNNFNDNGLI
SPDRVPNPHAYEVGYFYQNIWTTPADLSKGEINIYNENFFRDLSAFYLEWQLLANGEIIQ
NGIVSDLNVAPQQTAKLQLPFDIKNICSCKELLLNVSYKLKAAETLLPAGETIAYDQMSI
RDYKAPELKLENKQSSNIAVVVPSFQDNDHNYLIVSGEDFTLEFNKHNGYLCRYDVSGTQ
LMEDGSALTPNFWRAPTDNDFGAGLQHRYGAWKNPELKLTSLKHDIENEQAVVRAEYDMK
SIGGKLFLTYAINNKGAVKVTQKMEADKSKKVSDMFRFGMQLRMPVTFNEIEYYGRGPGE
NYSDRNHAARIGKYRQTVEEQFYPYIRPQETGTKTDIRWWRLLNIGGNGLQFVADAPFSA
SALNYTIESLDDGAGKDQRHSPEVEKANFTNFCIDKVQTGLACVNSWGAIALEKYRLPYQ
DYEFSFIMNPVYHKLK
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