SitesBLAST
Comparing Echvi_2143 FitnessBrowser__Cola:Echvi_2143 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: 29:1031/1036 of query aligns to 4:977/1083 of 6s6zA
3bgaA Crystal structure of beta-galactosidase from bacteroides thetaiotaomicron vpi-5482
37% identity, 97% coverage: 27:1035/1036 of query aligns to 2:994/1003 of 3bgaA
- active site: D201 (= D221), H354 (= H378), H387 (= H412), E412 (= E437), H414 (= H439), E458 (= E484), Y499 (= Y525), E522 (= E547), S584 (= S608), F588 (= F612), N591 (= N615)
- binding magnesium ion: E412 (= E437), H414 (= H439), E458 (= E484)
P00722 Beta-galactosidase; Beta-gal; Lactase; EC 3.2.1.23 from Escherichia coli (strain K12) (see 13 papers)
33% identity, 97% coverage: 29:1032/1036 of query aligns to 17:1020/1024 of P00722
- D202 (= D221) 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 (= H378) mutation H->D,F,L,N: Less stable to heat than wild-type. Causes significant destabilizations of the first transition state.
- H392 (= H412) mutation H->E,F,K: Essentially inactive unless very rapid purification. Causes very large destabilizations of the transition state.
- E417 (= E437) binding
- H419 (= H439) binding
- E462 (= E484) active site, Proton donor; binding ; mutation to H: Slowly inactivates galactosidase activity by reducing the binding of magnesium. It increases binding specificity.
- E538 (= E547) active site, Nucleophile; mutation to Q: 10000-fold decrease in the beta-galactosidase activity.
- H541 (= H550) mutation H->E,F,N: Poorly reactive with galactosyl substrates. Less stable to heat than wild-type.
- N598 (≠ S608) binding
- F602 (= F612) mutation to A: Decreases the stability of the loop 794-804.
- G795 (= G806) mutation to A: It forces the apoenzyme to adopt the closed rather than the open conformation. Reduces the binding affinity.
- E798 (≠ R809) 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 (= W1012) mutation W->F,G,L,T: Decreases affinity for substrate.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1jz6A E. Coli (lacz) beta-galactosidase in complex with galacto-tetrazole (see paper)
33% identity, 97% coverage: 29:1032/1036 of query aligns to 4:1007/1011 of 1jz6A
- active site: D189 (= D221), H345 (= H378), H379 (= H412), E404 (= E437), H406 (= H439), E449 (= E484), Y491 (= Y525), E525 (= E547), N585 (≠ S608), F589 (= F612), N592 (= N615)
- binding (5r, 6s, 7s, 8s)-5-hydroxymethyl-6,7,8-trihydroxy-tetrazolo[1,5-a]piperidine: D189 (= D221), H379 (= H412), E449 (= E484), Y491 (= Y525), E525 (= E547), H528 (= H550), W556 (= W578), N592 (= N615)
- binding magnesium ion: N6 (= N31), V9 (= V34), Q151 (≠ E183), D181 (= D213), E404 (= E437), H406 (= H439), E449 (= E484), S635 (≠ L659), E638 (≠ Y662), L658 (≠ F683)
- binding sodium ion: D189 (= D221), F544 (≠ I566), Y547 (= Y569), P548 (= P570), L550 (= L572), F589 (= F612), C590 (≠ L613), N592 (= N615), F919 (≠ R931), P920 (= P932), L955 (= L975), M956 (≠ Y976), T958 (≠ G978)
Sites not aligning to the query:
1jz5A E. Coli (lacz) beta-galactosidase in complex with d-galctopyranosyl-1- on (see paper)
33% identity, 97% coverage: 29:1032/1036 of query aligns to 4:1007/1011 of 1jz5A
- active site: D189 (= D221), H345 (= H378), H379 (= H412), E404 (= E437), H406 (= H439), E449 (= E484), Y491 (= Y525), E525 (= E547), N585 (≠ S608), F589 (= F612), N592 (= N615)
- binding D-galactonolactone: D189 (= D221), H379 (= H412), N448 (= N483), E449 (= E484), M490 (≠ Q524), Y491 (= Y525), E525 (= E547), H528 (= H550), W556 (= W578), F589 (= F612), N592 (= N615)
- binding magnesium ion: N6 (= N31), V9 (= V34), Q151 (≠ E183), D181 (= D213), E404 (= E437), H406 (= H439), E449 (= E484)
Sites not aligning to the query:
1jz3A E. Coli (lacz) beta-galactosidase-trapped 2-deoxy-galactosyl enzyme intermediate (see paper)
33% identity, 97% coverage: 29:1032/1036 of query aligns to 4:1007/1011 of 1jz3A
- active site: D189 (= D221), H345 (= H378), H379 (= H412), E404 (= E437), H406 (= H439), E449 (= E484), Y491 (= Y525), E525 (= E547), N585 (≠ S608), F589 (= F612), N592 (= N615)
- binding 2-deoxy-alpha-D-galactopyranose: D189 (= D221), H379 (= H412), E449 (= E484), Y491 (= Y525), E525 (= E547), H528 (= H550), W556 (= W578), F589 (= F612)
- binding magnesium ion: N6 (= N31), V9 (= V34), Q151 (≠ E183), D181 (= D213), E404 (= E437), H406 (= H439), E449 (= E484)
Sites not aligning to the query:
1jz2A E. Coli (lacz) beta-galactosidase-trapped 2-f-galactosyl-enzyme intermediate (orthorhombic) (see paper)
33% identity, 97% coverage: 29:1032/1036 of query aligns to 4:1007/1011 of 1jz2A
- active site: D189 (= D221), H345 (= H378), H379 (= H412), E404 (= E437), H406 (= H439), E449 (= E484), Y491 (= Y525), E525 (= E547), N585 (≠ S608), F589 (= F612), N592 (= N615)
- binding 2-deoxy-2-fluoro-beta-D-galactopyranose: D189 (= D221), H379 (= H412), N448 (= N483), E449 (= E484), Y491 (= Y525), E525 (= E547), H528 (= H550), W556 (= W578), F589 (= F612)
- binding magnesium ion: N6 (= N31), V9 (= V34), Q151 (≠ E183), D181 (= D213), E404 (= E437), H406 (= H439), E449 (= E484)
- binding sodium ion: D189 (= D221), F544 (≠ I566), Y547 (= Y569), P548 (= P570), L550 (= L572), Q551 (= Q573), F589 (= F612), N592 (= N615), F919 (≠ R931), P920 (= P932), L955 (= L975), M956 (≠ Y976), T958 (≠ G978)
Sites not aligning to the query:
1jyxA E. Coli (lacz) beta-galactosidase in complex with iptg (see paper)
33% identity, 97% coverage: 29:1032/1036 of query aligns to 4:1007/1011 of 1jyxA
- active site: D189 (= D221), H345 (= H378), H379 (= H412), E404 (= E437), H406 (= H439), E449 (= E484), Y491 (= Y525), E525 (= E547), N585 (≠ S608), F589 (= F612), N592 (= N615)
- binding 1-methylethyl 1-thio-beta-D-galactopyranoside: N90 (= N119), D189 (= D221), E292 (= E325), P294 (= P327), E449 (= E484), E525 (= E547), H528 (= H550), N592 (= N615), R633 (= R657), D636 (≠ S660), Q690 (= Q717), W696 (vs. gap), W987 (= W1012)
- binding magnesium ion: N6 (= N31), V9 (= V34), Q151 (≠ E183), D181 (= D213), E404 (= E437), H406 (= H439), E449 (= E484)
- binding sodium ion: D189 (= D221), F544 (≠ I566), Y547 (= Y569), P548 (= P570), L550 (= L572), Q551 (= Q573), F589 (= F612), C590 (≠ L613), N592 (= N615), F919 (≠ R931), P920 (= P932), L955 (= L975), M956 (≠ Y976), T958 (≠ G978)
Sites not aligning to the query:
6tshA Beta-galactosidase in complex with deoxygalacto-nojirimycin (see paper)
33% identity, 97% coverage: 29:1032/1036 of query aligns to 8:1011/1015 of 6tshA
- binding (2R,3S,4R,5S)-2-(hydroxymethyl)piperidine-3,4,5-triol: D193 (= D221), H383 (= H412), E453 (= E484), E529 (= E547), H532 (= H550), W560 (= W578), F593 (= F612)
- binding magnesium ion: E408 (= E437), H410 (= H439), E453 (= E484)
5a1aA 2.2 a resolution cryo-em structure of beta-galactosidase in complex with a cell-permeant inhibitor (see paper)
33% identity, 97% coverage: 29:1032/1036 of query aligns to 15:1018/1022 of 5a1aA
- active site: D200 (= D221), H356 (= H378), H390 (= H412), E415 (= E437), H417 (= H439), E460 (= E484), Y502 (= Y525), E536 (= E547), N596 (≠ S608), F600 (= F612), N603 (= N615)
- binding magnesium ion: W15 (≠ F29), N17 (= N31), V20 (= V34), Q162 (≠ E183), D192 (= D213), E415 (= E437), H417 (= H439), E460 (= E484)
- binding sodium ion: D200 (= D221), H539 (= H550), F555 (≠ I566), Y558 (= Y569), P559 (= P570), L561 (= L572), F600 (= F612), N603 (= N615)
- binding 2-phenylethyl 1-thio-beta-D-galactopyranoside: N101 (= N119), D200 (= D221), M501 (≠ Q524), Y502 (= Y525), H539 (= H550), D597 (= D609), F600 (= F612), W998 (= W1012)
Sites not aligning to the query:
1jywA E. Coli (lacz) beta-galactosidase (e537q) in complex with pnpg (see paper)
33% identity, 97% coverage: 29:1032/1036 of query aligns to 4:1007/1011 of 1jywA
- active site: D189 (= D221), H345 (= H378), H379 (= H412), E404 (= E437), H406 (= H439), E449 (= E484), Y491 (= Y525), Q525 (≠ E547), N585 (≠ S608), F589 (= F612), N592 (= N615)
- binding 4-nitrophenyl beta-D-galactopyranoside: N90 (= N119), D189 (= D221), E449 (= E484), Y491 (= Y525), Q525 (≠ E547), H528 (= H550), N592 (= N615), W987 (= W1012)
- binding magnesium ion: N6 (= N31), V9 (= V34), Q151 (≠ E183), D181 (= D213), E404 (= E437), H406 (= H439), E449 (= E484)
Sites not aligning to the query:
1jyvA E. Coli (lacz) beta-galactosidase (e537q) in complex with onpg (see paper)
33% identity, 97% coverage: 29:1032/1036 of query aligns to 4:1007/1011 of 1jyvA
- active site: D189 (= D221), H345 (= H378), H379 (= H412), E404 (= E437), H406 (= H439), E449 (= E484), Y491 (= Y525), Q525 (≠ E547), N585 (≠ S608), F589 (= F612), N592 (= N615)
- binding 2-nitrophenyl beta-D-galactopyranoside: N90 (= N119), N90 (= N119), V91 (≠ H120), D189 (= D221), H406 (= H439), E449 (= E484), Y491 (= Y525), H528 (= H550), D586 (= D609), F589 (= F612), N592 (= N615), V783 (≠ G807), V783 (≠ G807), E785 (≠ R809), R788 (≠ K812), W987 (= W1012)
- binding magnesium ion: N6 (= N31), V9 (= V34), Q151 (≠ E183), D181 (= D213), E404 (= E437), H406 (= H439), E449 (= E484)
Sites not aligning to the query:
1jynA E. Coli (lacz) beta-galactosidase (e537q) in complex with lactose (see paper)
33% identity, 97% coverage: 29:1032/1036 of query aligns to 4:1007/1011 of 1jynA
- active site: D189 (= D221), H345 (= H378), H379 (= H412), E404 (= E437), H406 (= H439), E449 (= E484), Y491 (= Y525), Q525 (≠ E547), N585 (≠ S608), F589 (= F612), N592 (= N615)
- binding beta-D-glucopyranose: N90 (= N119), W987 (= W1012)
- binding beta-D-galactopyranose: N90 (= N119), D189 (= D221), E449 (= E484), Y491 (= Y525), H528 (= H550), N592 (= N615), W987 (= W1012)
- binding magnesium ion: N6 (= N31), V9 (= V34), Q151 (≠ E183), D181 (= D213), E404 (= E437), H406 (= H439), E449 (= E484)
- binding sodium ion: D189 (= D221), F544 (≠ I566), Y547 (= Y569), P548 (= P570), L550 (= L572), F589 (= F612), N592 (= N615), S635 (≠ L659), D636 (≠ S660), E638 (≠ Y662), L658 (≠ F683), F919 (≠ R931), P920 (= P932), L955 (= L975), M956 (≠ Y976), T958 (≠ G978)
Sites not aligning to the query:
7btkC E.Coli beta-galactosidase (e537q) in complex with fluorescent probe ksa01 (see paper)
33% identity, 97% coverage: 29:1032/1036 of query aligns to 16:1019/1023 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 (= N119), D201 (= D221), H391 (= H412), N460 (= N483), E461 (= E484), Y503 (= Y525), F512 (vs. gap), Q537 (≠ E547), W568 (= W578), W999 (= W1012)
- binding magnesium ion: N18 (= N31), V21 (= V34), Q163 (≠ E183), D193 (= D213), D201 (= D221), E416 (= E437), H418 (= H439), E461 (= E484)
Sites not aligning to the query:
7brsA E.Coli beta-galactosidase (e537q) in complex with fluorescent probe ksa02 (see paper)
33% identity, 97% coverage: 29:1032/1036 of query aligns to 14:1017/1021 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 (= N119), D199 (= D221), E459 (= E484), Y501 (= Y525), Q535 (≠ E547), H538 (= H550), N602 (= N615), W997 (= W1012)
- binding magnesium ion: N16 (= N31), V19 (= V34), Q161 (≠ E183), D191 (= D213), E414 (= E437), H416 (= H439), E459 (= E484)
Sites not aligning to the query:
6kuzA E.Coli beta-galactosidase (e537q) in complex with fluorescent probe ksl01 (see paper)
33% identity, 97% coverage: 29:1032/1036 of query aligns to 14:1017/1021 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 (= N119), D199 (= D221), H389 (= H412), H416 (= H439), E459 (= E484), Y501 (= Y525), Q535 (≠ E547), H538 (= H550), W566 (= W578), W997 (= W1012)
- binding magnesium ion: N16 (= N31), V19 (= V34), Q161 (≠ E183), D191 (= D213), E414 (= E437), H416 (= H439), E459 (= E484)
Sites not aligning to the query:
4duxA E. Coli (lacz) beta-galactosidase (n460s) in complex with l-ribose (see paper)
33% identity, 97% coverage: 29:1032/1036 of query aligns to 8:1011/1015 of 4duxA
- active site: D193 (= D221), H349 (= H378), H383 (= H412), E408 (= E437), H410 (= H439), E453 (= E484), Y495 (= Y525), E529 (= E547), N589 (≠ S608), F593 (= F612), N596 (= N615)
- binding beta-L-ribopyranose: D193 (= D221), H383 (= H412), E453 (= E484), M494 (≠ Q524), Y495 (= Y525), E529 (= E547), H532 (= H550), W560 (= W578), F593 (= F612), S788 (≠ G808), W991 (= W1012)
- binding magnesium ion: N10 (= N31), V13 (= V34), Q155 (≠ E183), D185 (= D213), E408 (= E437), H410 (= H439), E453 (= E484)
Sites not aligning to the query:
P06864 Evolved beta-galactosidase subunit alpha; Beta-gal; Lactase; EC 3.2.1.23 from Escherichia coli (strain K12) (see paper)
31% identity, 97% coverage: 29:1035/1036 of query aligns to 4:999/1030 of P06864
- E449 (= E484) active site, Proton donor
1yq2A Beta-galactosidase from arthrobacter sp. C2-2 (isoenzyme c2-2-1) (see paper)
30% identity, 93% coverage: 67:1025/1036 of query aligns to 30:1014/1020 of 1yq2A
- active site: D198 (= D221), H332 (= H378), H366 (= H412), E391 (= E437), H393 (= H439), E439 (= E484), Y480 (= Y525), E518 (= E547), H578 (≠ S608), F582 (= F612), D585 (≠ N615)
- binding magnesium ion: A522 (= A551), G524 (= G553), G526 (≠ S555)
3obaA Structure of the beta-galactosidase from kluyveromyces lactis (see paper)
30% identity, 97% coverage: 29:1034/1036 of query aligns to 8:1022/1024 of 3obaA
- active site: D186 (= D221), H354 (= H378), H388 (= H412), E413 (= E437), H415 (= H439), E481 (= E484), Y522 (= Y525), E550 (= E547), H615 (≠ S608), F619 (= F612), D622 (≠ N615)
- binding manganese (iii) ion: D592 (vs. gap), H974 (= H985), D977 (≠ E988)
Query Sequence
>Echvi_2143 FitnessBrowser__Cola:Echvi_2143
MKSIITSLFCAFICVIKVSGQDRKADPIFENPHVQEENRLPMRASYFPYENEALAEKGEK
AASDRFFDLNGTWKFFWTDHYTKLPKDFYATGFDDAAWDDFQVPANWEFNGYGTPIYVNH
PFEFAVDNPNPPFIENEKNPAGVYRRKISLPDGWEDQQVFIHLGAVKSAFRLYVNGVYVG
LGEDSKLESEFELTDYVQPGENLITIEVRRWHDGSYLEAQDFWRISGIERDVYLYSRPKV
HFYDLFVKSPLTNSYRDGKLDVTVDLWNRTDEQQGENTVMAKLLDPNGNVVFEQTQATIG
LKRKQGKTVLNFATEIPSVKAWSAETPTLYQLELVLANAAGEPLEVVRQNVGFRTYEVVG
NQFLVNGKAVLFKGVNRHESHPETHHVITKEQMETDVRIMKELNMNAVRLSHYPNDPYWY
ELCDKYGFYVIDEANIESHGMYYSPERTLGNAPEWLHAHMLRIKRMVFRDKNHPSVVAWS
MGNEAGNGYNFYKAYEWIKAYDPSRPVQYERSTYEWNTDIIVPQYPHPNSMIRYAESNPK
RPYIMSEYAHAMGNSMGNFREYWEVIKAYPMLQGGYIWDWVDQGIYKEIDGKRVFGYGGD
WGPEGTPSDDNFLINGVIMADRRWNPHAYEVRRVHQEVSFELTEDDRLEIFNEYFFRDLS
NYTFEAILLKNGEVIKRASIGTFALAPRQHTVVDLPFGLVRDESAEYRLQVEGRIVQEEG
RMAPKTLLAEAEFALTDPVLKKFDPQAADVEVREEAGKLWISNKKFSVFFNVATGQFHDY
KVGKNTLIVDGPSLSLFRPLVDNDFGGGRGSKLDYQHGKVTSLQKLEHQAAADGTYQVKA
IYEVLGGDASFEQVYRFDDGGKIRVDNTFKAIKGDHDYLLKIGTDLKLPGALDQFKWYGR
GPWESYADRKYSAQVGLYEGSVMEQYHPYVRPQESGNKTDVRWASVSKSQNEGLMIYALE
DLLNVSALPYGIDQLYPGKEKQNIHSGELEPNGYTNLHVDLEQTGVAGINSWGSIALEAY
RVSFKDYAFSYVIAPF
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