SitesBLAST
Comparing Echvi_0485 FitnessBrowser__Cola:Echvi_0485 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)
40% identity, 97% coverage: 27:1038/1038 of query aligns to 3:983/1083 of 6s6zA
3bgaA Crystal structure of beta-galactosidase from bacteroides thetaiotaomicron vpi-5482
38% identity, 97% coverage: 27:1031/1038 of query aligns to 3:991/1003 of 3bgaA
- active site: D201 (= D217), H354 (= H369), H387 (= H403), E412 (= E428), H414 (= H430), E458 (= E481), Y499 (= Y522), E522 (= E545), S584 (≠ N607), F588 (= F611), N591 (= N614)
- binding magnesium ion: E412 (= E428), H414 (= H430), E458 (= E481)
P06864 Evolved beta-galactosidase subunit alpha; Beta-gal; Lactase; EC 3.2.1.23 from Escherichia coli (strain K12) (see paper)
33% identity, 97% coverage: 26:1034/1038 of query aligns to 2:997/1030 of P06864
- E449 (= E481) active site, Proton donor
P00722 Beta-galactosidase; Beta-gal; Lactase; EC 3.2.1.23 from Escherichia coli (strain K12) (see 13 papers)
34% identity, 97% coverage: 25:1033/1038 of query aligns to 14:1020/1024 of P00722
- D202 (= D217) 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 (= H369) mutation H->D,F,L,N: Less stable to heat than wild-type. Causes significant destabilizations of the first transition state.
- H392 (= H403) mutation H->E,F,K: Essentially inactive unless very rapid purification. Causes very large destabilizations of the transition state.
- E417 (= E428) binding
- H419 (= H430) binding
- E462 (= E481) active site, Proton donor; binding ; mutation to H: Slowly inactivates galactosidase activity by reducing the binding of magnesium. It increases binding specificity.
- E538 (= E545) active site, Nucleophile; mutation to Q: 10000-fold decrease in the beta-galactosidase activity.
- H541 (= H548) mutation H->E,F,N: Poorly reactive with galactosyl substrates. Less stable to heat than wild-type.
- N598 (= N607) binding
- F602 (= F611) mutation to A: Decreases the stability of the loop 794-804.
- G795 (= G805) mutation to A: It forces the apoenzyme to adopt the closed rather than the open conformation. Reduces the binding affinity.
- E798 (≠ M808) 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 (= W1013) mutation W->F,G,L,T: Decreases affinity for substrate.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5a1aA 2.2 a resolution cryo-em structure of beta-galactosidase in complex with a cell-permeant inhibitor (see paper)
34% identity, 97% coverage: 25:1033/1038 of query aligns to 12:1018/1022 of 5a1aA
- active site: D200 (= D217), H356 (= H369), H390 (= H403), E415 (= E428), H417 (= H430), E460 (= E481), Y502 (= Y522), E536 (= E545), N596 (= N607), F600 (= F611), N603 (= N614)
- binding magnesium ion: D14 (≠ E27), W15 (= W28), N17 (≠ D30), V20 (≠ A33), Q162 (≠ K179), D192 (= D209), E415 (= E428), H417 (= H430), E460 (= E481)
- binding sodium ion: D200 (= D217), H539 (= H548), F555 (≠ I564), Y558 (≠ S567), P559 (= P568), L561 (≠ M570), F600 (= F611), N603 (= N614)
- binding 2-phenylethyl 1-thio-beta-D-galactopyranoside: N101 (= N118), D200 (= D217), M501 (= M521), Y502 (= Y522), H539 (= H548), D597 (= D608), F600 (= F611), W998 (= W1013)
6tshA Beta-galactosidase in complex with deoxygalacto-nojirimycin (see paper)
34% identity, 97% coverage: 25:1033/1038 of query aligns to 5:1011/1015 of 6tshA
- binding (2R,3S,4R,5S)-2-(hydroxymethyl)piperidine-3,4,5-triol: D193 (= D217), H383 (= H403), E453 (= E481), E529 (= E545), H532 (= H548), W560 (= W576), F593 (= F611)
- binding magnesium ion: E408 (= E428), H410 (= H430), E453 (= E481)
7btkC E.Coli beta-galactosidase (e537q) in complex with fluorescent probe ksa01 (see paper)
34% identity, 97% coverage: 25:1033/1038 of query aligns to 13:1019/1023 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 (= N118), D201 (= D217), H391 (= H403), N460 (= N480), E461 (= E481), Y503 (= Y522), F512 (vs. gap), Q537 (≠ E545), W568 (= W576), W999 (= W1013)
- binding magnesium ion: D15 (≠ E27), N18 (≠ D30), V21 (≠ A33), Q163 (≠ K179), D193 (= D209), D201 (= D217), E416 (= E428), H418 (= H430), E461 (= E481)
7brsA E.Coli beta-galactosidase (e537q) in complex with fluorescent probe ksa02 (see paper)
34% identity, 97% coverage: 25:1033/1038 of query aligns to 11:1017/1021 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 (= N118), D199 (= D217), E459 (= E481), Y501 (= Y522), Q535 (≠ E545), H538 (= H548), N602 (= N614), W997 (= W1013)
- binding magnesium ion: D13 (≠ E27), N16 (≠ D30), V19 (≠ A33), Q161 (≠ K179), D191 (= D209), E414 (= E428), H416 (= H430), E459 (= E481)
6kuzA E.Coli beta-galactosidase (e537q) in complex with fluorescent probe ksl01 (see paper)
34% identity, 97% coverage: 25:1033/1038 of query aligns to 11:1017/1021 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 (= N118), D199 (= D217), H389 (= H403), H416 (= H430), E459 (= E481), Y501 (= Y522), Q535 (≠ E545), H538 (= H548), W566 (= W576), W997 (= W1013)
- binding magnesium ion: D13 (≠ E27), N16 (≠ D30), V19 (≠ A33), Q161 (≠ K179), D191 (= D209), E414 (= E428), H416 (= H430), E459 (= E481)
1jz6A E. Coli (lacz) beta-galactosidase in complex with galacto-tetrazole (see paper)
34% identity, 97% coverage: 25:1033/1038 of query aligns to 1:1007/1011 of 1jz6A
- active site: D189 (= D217), H345 (= H369), H379 (= H403), E404 (= E428), H406 (= H430), E449 (= E481), Y491 (= Y522), E525 (= E545), N585 (= N607), F589 (= F611), N592 (= N614)
- binding (5r, 6s, 7s, 8s)-5-hydroxymethyl-6,7,8-trihydroxy-tetrazolo[1,5-a]piperidine: D189 (= D217), H379 (= H403), E449 (= E481), Y491 (= Y522), E525 (= E545), H528 (= H548), W556 (= W576), N592 (= N614)
- binding magnesium ion: D3 (≠ E27), N6 (≠ D30), V9 (≠ A33), Q151 (≠ K179), D181 (= D209), E404 (= E428), H406 (= H430), E449 (= E481), S635 (≠ L658), E638 (≠ Y661), L658 (≠ V681)
- binding sodium ion: D189 (= D217), F544 (≠ I564), Y547 (≠ S567), P548 (= P568), L550 (≠ M570), F589 (= F611), C590 (= C612), N592 (= N614), F919 (≠ R933), P920 (= P934), L955 (= L976), M956 (≠ K982), T958 (≠ Q984)
1jz5A E. Coli (lacz) beta-galactosidase in complex with d-galctopyranosyl-1- on (see paper)
34% identity, 97% coverage: 25:1033/1038 of query aligns to 1:1007/1011 of 1jz5A
- active site: D189 (= D217), H345 (= H369), H379 (= H403), E404 (= E428), H406 (= H430), E449 (= E481), Y491 (= Y522), E525 (= E545), N585 (= N607), F589 (= F611), N592 (= N614)
- binding D-galactonolactone: D189 (= D217), H379 (= H403), N448 (= N480), E449 (= E481), M490 (= M521), Y491 (= Y522), E525 (= E545), H528 (= H548), W556 (= W576), F589 (= F611), N592 (= N614)
- binding magnesium ion: D3 (≠ E27), N6 (≠ D30), V9 (≠ A33), Q151 (≠ K179), D181 (= D209), E404 (= E428), H406 (= H430), E449 (= E481)
1jz3A E. Coli (lacz) beta-galactosidase-trapped 2-deoxy-galactosyl enzyme intermediate (see paper)
34% identity, 97% coverage: 25:1033/1038 of query aligns to 1:1007/1011 of 1jz3A
- active site: D189 (= D217), H345 (= H369), H379 (= H403), E404 (= E428), H406 (= H430), E449 (= E481), Y491 (= Y522), E525 (= E545), N585 (= N607), F589 (= F611), N592 (= N614)
- binding 2-deoxy-alpha-D-galactopyranose: D189 (= D217), H379 (= H403), E449 (= E481), Y491 (= Y522), E525 (= E545), H528 (= H548), W556 (= W576), F589 (= F611)
- binding magnesium ion: D3 (≠ E27), N6 (≠ D30), V9 (≠ A33), Q151 (≠ K179), D181 (= D209), E404 (= E428), H406 (= H430), E449 (= E481)
1jz2A E. Coli (lacz) beta-galactosidase-trapped 2-f-galactosyl-enzyme intermediate (orthorhombic) (see paper)
34% identity, 97% coverage: 25:1033/1038 of query aligns to 1:1007/1011 of 1jz2A
- active site: D189 (= D217), H345 (= H369), H379 (= H403), E404 (= E428), H406 (= H430), E449 (= E481), Y491 (= Y522), E525 (= E545), N585 (= N607), F589 (= F611), N592 (= N614)
- binding 2-deoxy-2-fluoro-beta-D-galactopyranose: D189 (= D217), H379 (= H403), N448 (= N480), E449 (= E481), Y491 (= Y522), E525 (= E545), H528 (= H548), W556 (= W576), F589 (= F611)
- binding magnesium ion: D3 (≠ E27), N6 (≠ D30), V9 (≠ A33), Q151 (≠ K179), D181 (= D209), E404 (= E428), H406 (= H430), E449 (= E481)
- binding sodium ion: D189 (= D217), F544 (≠ I564), Y547 (≠ S567), P548 (= P568), L550 (≠ M570), Q551 (= Q571), F589 (= F611), N592 (= N614), F919 (≠ R933), P920 (= P934), L955 (= L976), M956 (≠ K982), T958 (≠ Q984)
1jyxA E. Coli (lacz) beta-galactosidase in complex with iptg (see paper)
34% identity, 97% coverage: 25:1033/1038 of query aligns to 1:1007/1011 of 1jyxA
- active site: D189 (= D217), H345 (= H369), H379 (= H403), E404 (= E428), H406 (= H430), E449 (= E481), Y491 (= Y522), E525 (= E545), N585 (= N607), F589 (= F611), N592 (= N614)
- binding 1-methylethyl 1-thio-beta-D-galactopyranoside: N90 (= N118), D189 (= D217), E292 (= E316), P294 (= P318), E449 (= E481), E525 (= E545), H528 (= H548), N592 (= N614), R633 (≠ T656), D636 (= D659), Q690 (≠ T711), W696 (≠ L717), W987 (= W1013)
- binding magnesium ion: D3 (≠ E27), N6 (≠ D30), V9 (≠ A33), Q151 (≠ K179), D181 (= D209), E404 (= E428), H406 (= H430), E449 (= E481)
- binding sodium ion: D189 (= D217), F544 (≠ I564), Y547 (≠ S567), P548 (= P568), L550 (≠ M570), Q551 (= Q571), F589 (= F611), C590 (= C612), N592 (= N614), F919 (≠ R933), P920 (= P934), L955 (= L976), M956 (≠ K982), T958 (≠ Q984)
1jywA E. Coli (lacz) beta-galactosidase (e537q) in complex with pnpg (see paper)
34% identity, 97% coverage: 25:1033/1038 of query aligns to 1:1007/1011 of 1jywA
- active site: D189 (= D217), H345 (= H369), H379 (= H403), E404 (= E428), H406 (= H430), E449 (= E481), Y491 (= Y522), Q525 (≠ E545), N585 (= N607), F589 (= F611), N592 (= N614)
- binding 4-nitrophenyl beta-D-galactopyranoside: N90 (= N118), D189 (= D217), E449 (= E481), Y491 (= Y522), Q525 (≠ E545), H528 (= H548), N592 (= N614), W987 (= W1013)
- binding magnesium ion: D3 (≠ E27), N6 (≠ D30), V9 (≠ A33), Q151 (≠ K179), D181 (= D209), E404 (= E428), H406 (= H430), E449 (= E481)
1jyvA E. Coli (lacz) beta-galactosidase (e537q) in complex with onpg (see paper)
34% identity, 97% coverage: 25:1033/1038 of query aligns to 1:1007/1011 of 1jyvA
- active site: D189 (= D217), H345 (= H369), H379 (= H403), E404 (= E428), H406 (= H430), E449 (= E481), Y491 (= Y522), Q525 (≠ E545), N585 (= N607), F589 (= F611), N592 (= N614)
- binding 2-nitrophenyl beta-D-galactopyranoside: N90 (= N118), N90 (= N118), V91 (= V119), D189 (= D217), H406 (= H430), E449 (= E481), Y491 (= Y522), H528 (= H548), D586 (= D608), F589 (= F611), N592 (= N614), V783 (≠ N806), V783 (≠ N806), E785 (≠ M808), R788 (= R811), W987 (= W1013)
- binding magnesium ion: D3 (≠ E27), N6 (≠ D30), V9 (≠ A33), Q151 (≠ K179), D181 (= D209), E404 (= E428), H406 (= H430), E449 (= E481)
1jynA E. Coli (lacz) beta-galactosidase (e537q) in complex with lactose (see paper)
34% identity, 97% coverage: 25:1033/1038 of query aligns to 1:1007/1011 of 1jynA
- active site: D189 (= D217), H345 (= H369), H379 (= H403), E404 (= E428), H406 (= H430), E449 (= E481), Y491 (= Y522), Q525 (≠ E545), N585 (= N607), F589 (= F611), N592 (= N614)
- binding beta-D-glucopyranose: N90 (= N118), W987 (= W1013)
- binding beta-D-galactopyranose: N90 (= N118), D189 (= D217), E449 (= E481), Y491 (= Y522), H528 (= H548), N592 (= N614), W987 (= W1013)
- binding magnesium ion: D3 (≠ E27), N6 (≠ D30), V9 (≠ A33), Q151 (≠ K179), D181 (= D209), E404 (= E428), H406 (= H430), E449 (= E481)
- binding sodium ion: D189 (= D217), F544 (≠ I564), Y547 (≠ S567), P548 (= P568), L550 (≠ M570), F589 (= F611), N592 (= N614), S635 (≠ L658), D636 (= D659), E638 (≠ Y661), L658 (≠ V681), F919 (≠ R933), P920 (= P934), L955 (= L976), M956 (≠ K982), T958 (≠ Q984)
4duxA E. Coli (lacz) beta-galactosidase (n460s) in complex with l-ribose (see paper)
34% identity, 97% coverage: 25:1033/1038 of query aligns to 5:1011/1015 of 4duxA
- active site: D193 (= D217), H349 (= H369), H383 (= H403), E408 (= E428), H410 (= H430), E453 (= E481), Y495 (= Y522), E529 (= E545), N589 (= N607), F593 (= F611), N596 (= N614)
- binding beta-L-ribopyranose: D193 (= D217), H383 (= H403), E453 (= E481), M494 (= M521), Y495 (= Y522), E529 (= E545), H532 (= H548), W560 (= W576), F593 (= F611), S788 (≠ H807), W991 (= W1013)
- binding magnesium ion: D7 (≠ E27), N10 (≠ D30), V13 (≠ A33), Q155 (≠ K179), D185 (= D209), E408 (= E428), H410 (= H430), E453 (= E481)
1yq2A Beta-galactosidase from arthrobacter sp. C2-2 (isoenzyme c2-2-1) (see paper)
32% identity, 88% coverage: 91:1008/1038 of query aligns to 67:992/1020 of 1yq2A
- active site: D198 (= D217), H332 (= H369), H366 (= H403), E391 (= E428), H393 (= H430), E439 (= E481), Y480 (= Y522), E518 (= E545), H578 (≠ N607), F582 (= F611), D585 (≠ N614)
- binding magnesium ion: A522 (≠ S549), G524 (= G551), G526 (≠ S553)
3obaA Structure of the beta-galactosidase from kluyveromyces lactis (see paper)
31% identity, 97% coverage: 30:1032/1038 of query aligns to 10:1019/1024 of 3obaA
- active site: D186 (= D217), H354 (= H369), H388 (= H403), E413 (= E428), H415 (= H430), E481 (= E481), Y522 (= Y522), E550 (= E545), H615 (≠ N607), F619 (= F611), D622 (≠ N614)
- binding manganese (iii) ion: D592 (= D587), H974 (= H986), D977 (= D989)
Query Sequence
>Echvi_0485 FitnessBrowser__Cola:Echvi_0485
MQFKKLWMTGALVAALGGLLHAQSQNEWEDPTAVDRNKEAARAYFITYPSEEKALLGNRT
TNESFKTLDGLWKFSLVKRPQDRPTDFFEPTFKDEDWDDITVPSNWELEGYDMPVYTNVA
YPFPADPPLVDNQYNPVGTYRRTFSIPSQWDNQEVILHFGSISGYATVYVNGEEVGMTKA
AKTPAEFVITDYLKTGENTLAVQVFRWHDGSYLEDQDFWRLSGIERSVFLQAVPKLTIWD
FFVKSGLDDRYKNGVLEAAIQLRAFEGSDVQGGELSFELQDEDGKQVYSDTKAVSNGDQE
VKFSKTIGNVNKWSAEEPYLYQYTISLKDSRGRTLAAVSKKTGFRKVEIKDAQLMVNGQS
VLVKGVNRHEHHGVKGHVPDEEIMLRDIQLMKQNNINAVRMSHYPHSPRWYELCDEYGLY
VVDEANIETHGMGAEWQGRFKKDRHPAYLEAWAPAHLDRIHRLVERDKNHPSIIIWSMGN
ECGNGPVFYEAYNWMKERDDSRLVQFEQAGENEDTDIVCPMYPSIRHMQEYADATDKTRP
FIMCEYAHSMGNSTGNFQEYWDIILDSPHMQGGFIWDWVDQGLLAKDDNGKEFWAYGGDL
GGYFFQNDENFCANGLVTADRKPHPALHEVKKVYQDILFDYSPEKGLHVQNLFDFTNLDQ
YAFKWEWVEEGEVVKTGDFDVDLSADEEKYVQLNLPSVGDAETFLNVYAYTKNTEALVPA
GHEVAREQFALNEGYYFDHLEAVTGNLQVEQTEDLLTFATDKVTGAFDLKRGNFRKYTLK
DGEPWMVRSLPSPYFWRAPIDNDFGNHMPSRLGVWRSAHLGQKVLDVQVGEKSDEGIQIT
VNYELTNINVPYTVTYQIQSDGAVKVTAAMDLEGRDLPELPRYGMRMELPGQYGNLAYYG
RGPWENYSDRKHSSFIGQYNDQVENQFYWDYVRPQESGNKTDVRWLTLRNDKGQGIQIQG
IQPLSFSALDVSVEDLDPGLTKKQQHPTDIKPKNTVYLHIDWKQRGLGGDTSWGAYPHKP
YRLEDDHYEYSYVIRLVE
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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