SitesBLAST
Comparing CA265_RS04025 FitnessBrowser__Pedo557:CA265_RS04025 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)
3bgaA Crystal structure of beta-galactosidase from bacteroides thetaiotaomicron vpi-5482
40% identity, 98% coverage: 23:1054/1054 of query aligns to 1:996/1003 of 3bgaA
- active site: D201 (= D225), H354 (= H387), H387 (= H421), E412 (= E446), H414 (= H448), E458 (= E493), Y499 (= Y533), E522 (= E556), S584 (= S621), F588 (= F625), N591 (≠ K628)
- binding magnesium ion: E412 (= E446), H414 (= H448), E458 (= E493)
6s6zA Structure of beta-galactosidase from thermotoga maritima (see paper)
37% identity, 98% coverage: 24:1051/1054 of query aligns to 1:980/1083 of 6s6zA
P00722 Beta-galactosidase; Beta-gal; Lactase; EC 3.2.1.23 from Escherichia coli (strain K12) (see 13 papers)
33% identity, 97% coverage: 28:1046/1054 of query aligns to 18:1017/1024 of P00722
- D202 (= D225) 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 (= H387) mutation H->D,F,L,N: Less stable to heat than wild-type. Causes significant destabilizations of the first transition state.
- H392 (= H421) mutation H->E,F,K: Essentially inactive unless very rapid purification. Causes very large destabilizations of the transition state.
- E417 (= E446) binding
- H419 (= H448) binding
- E462 (= E493) active site, Proton donor; binding ; mutation to H: Slowly inactivates galactosidase activity by reducing the binding of magnesium. It increases binding specificity.
- E538 (= E556) active site, Nucleophile; mutation to Q: 10000-fold decrease in the beta-galactosidase activity.
- H541 (= H559) mutation H->E,F,N: Poorly reactive with galactosyl substrates. Less stable to heat than wild-type.
- N598 (≠ S621) binding
- F602 (= F625) mutation to A: Decreases the stability of the loop 794-804.
- G795 (= G820) mutation to A: It forces the apoenzyme to adopt the closed rather than the open conformation. Reduces the binding affinity.
- E798 (≠ L823) 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 (= W1029) 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)
33% identity, 97% coverage: 28:1046/1054 of query aligns to 9:1008/1015 of 6tshA
- binding (2R,3S,4R,5S)-2-(hydroxymethyl)piperidine-3,4,5-triol: D193 (= D225), H383 (= H421), E453 (= E493), E529 (= E556), H532 (= H559), W560 (= W587), F593 (= F625)
- binding magnesium ion: E408 (= E446), H410 (= H448), E453 (= E493)
5a1aA 2.2 a resolution cryo-em structure of beta-galactosidase in complex with a cell-permeant inhibitor (see paper)
33% identity, 97% coverage: 28:1046/1054 of query aligns to 16:1015/1022 of 5a1aA
- active site: D200 (= D225), H356 (= H387), H390 (= H421), E415 (= E446), H417 (= H448), E460 (= E493), Y502 (= Y533), E536 (= E556), N596 (≠ S621), F600 (= F625), N603 (≠ K628)
- binding magnesium ion: N17 (≠ T29), V20 (= V32), Q162 (≠ E187), D192 (= D217), E415 (= E446), H417 (= H448), E460 (= E493)
- binding sodium ion: D200 (= D225), H539 (= H559), F555 (≠ I575), Y558 (≠ N578), P559 (= P579), L561 (= L581), F600 (= F625), N603 (≠ K628)
- binding 2-phenylethyl 1-thio-beta-D-galactopyranoside: N101 (= N117), D200 (= D225), M501 (≠ Q532), Y502 (= Y533), H539 (= H559), D597 (= D622), F600 (= F625), W998 (= W1029)
Sites not aligning to the query:
1jz6A E. Coli (lacz) beta-galactosidase in complex with galacto-tetrazole (see paper)
33% identity, 97% coverage: 28:1046/1054 of query aligns to 5:1004/1011 of 1jz6A
- active site: D189 (= D225), H345 (= H387), H379 (= H421), E404 (= E446), H406 (= H448), E449 (= E493), Y491 (= Y533), E525 (= E556), N585 (≠ S621), F589 (= F625), N592 (≠ K628)
- binding (5r, 6s, 7s, 8s)-5-hydroxymethyl-6,7,8-trihydroxy-tetrazolo[1,5-a]piperidine: D189 (= D225), H379 (= H421), E449 (= E493), Y491 (= Y533), E525 (= E556), H528 (= H559), W556 (= W587), N592 (≠ K628)
- binding magnesium ion: N6 (≠ T29), V9 (= V32), Q151 (≠ E187), D181 (= D217), E404 (= E446), H406 (= H448), E449 (= E493), S635 (≠ I672), E638 (≠ V675), L658 (= L696)
- binding sodium ion: D189 (= D225), F544 (≠ I575), Y547 (≠ N578), P548 (= P579), L550 (= L581), F589 (= F625), C590 (= C626), N592 (≠ K628), F919 (≠ R948), P920 (= P949), L955 (= L992), M956 (≠ D993), T958 (≠ E995)
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: 28:1046/1054 of query aligns to 5:1004/1011 of 1jz5A
- active site: D189 (= D225), H345 (= H387), H379 (= H421), E404 (= E446), H406 (= H448), E449 (= E493), Y491 (= Y533), E525 (= E556), N585 (≠ S621), F589 (= F625), N592 (≠ K628)
- binding D-galactonolactone: D189 (= D225), H379 (= H421), N448 (= N492), E449 (= E493), M490 (≠ Q532), Y491 (= Y533), E525 (= E556), H528 (= H559), W556 (= W587), F589 (= F625), N592 (≠ K628)
- binding magnesium ion: N6 (≠ T29), V9 (= V32), Q151 (≠ E187), D181 (= D217), E404 (= E446), H406 (= H448), E449 (= E493)
Sites not aligning to the query:
1jz3A E. Coli (lacz) beta-galactosidase-trapped 2-deoxy-galactosyl enzyme intermediate (see paper)
33% identity, 97% coverage: 28:1046/1054 of query aligns to 5:1004/1011 of 1jz3A
- active site: D189 (= D225), H345 (= H387), H379 (= H421), E404 (= E446), H406 (= H448), E449 (= E493), Y491 (= Y533), E525 (= E556), N585 (≠ S621), F589 (= F625), N592 (≠ K628)
- binding 2-deoxy-alpha-D-galactopyranose: D189 (= D225), H379 (= H421), E449 (= E493), Y491 (= Y533), E525 (= E556), H528 (= H559), W556 (= W587), F589 (= F625)
- binding magnesium ion: N6 (≠ T29), V9 (= V32), Q151 (≠ E187), D181 (= D217), E404 (= E446), H406 (= H448), E449 (= E493)
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: 28:1046/1054 of query aligns to 5:1004/1011 of 1jz2A
- active site: D189 (= D225), H345 (= H387), H379 (= H421), E404 (= E446), H406 (= H448), E449 (= E493), Y491 (= Y533), E525 (= E556), N585 (≠ S621), F589 (= F625), N592 (≠ K628)
- binding 2-deoxy-2-fluoro-beta-D-galactopyranose: D189 (= D225), H379 (= H421), N448 (= N492), E449 (= E493), Y491 (= Y533), E525 (= E556), H528 (= H559), W556 (= W587), F589 (= F625)
- binding magnesium ion: N6 (≠ T29), V9 (= V32), Q151 (≠ E187), D181 (= D217), E404 (= E446), H406 (= H448), E449 (= E493)
- binding sodium ion: D189 (= D225), F544 (≠ I575), Y547 (≠ N578), P548 (= P579), L550 (= L581), Q551 (= Q582), F589 (= F625), N592 (≠ K628), F919 (≠ R948), P920 (= P949), L955 (= L992), M956 (≠ D993), T958 (≠ E995)
Sites not aligning to the query:
1jyxA E. Coli (lacz) beta-galactosidase in complex with iptg (see paper)
33% identity, 97% coverage: 28:1046/1054 of query aligns to 5:1004/1011 of 1jyxA
- active site: D189 (= D225), H345 (= H387), H379 (= H421), E404 (= E446), H406 (= H448), E449 (= E493), Y491 (= Y533), E525 (= E556), N585 (≠ S621), F589 (= F625), N592 (≠ K628)
- binding 1-methylethyl 1-thio-beta-D-galactopyranoside: N90 (= N117), D189 (= D225), E292 (= E334), P294 (= P336), E449 (= E493), E525 (= E556), H528 (= H559), N592 (≠ K628), R633 (≠ K670), D636 (≠ S673), Q690 (≠ L728), W696 (≠ F734), W987 (= W1029)
- binding magnesium ion: N6 (≠ T29), V9 (= V32), Q151 (≠ E187), D181 (= D217), E404 (= E446), H406 (= H448), E449 (= E493)
- binding sodium ion: D189 (= D225), F544 (≠ I575), Y547 (≠ N578), P548 (= P579), L550 (= L581), Q551 (= Q582), F589 (= F625), C590 (= C626), N592 (≠ K628), F919 (≠ R948), P920 (= P949), L955 (= L992), M956 (≠ D993), T958 (≠ E995)
Sites not aligning to the query:
7btkC E.Coli beta-galactosidase (e537q) in complex with fluorescent probe ksa01 (see paper)
33% identity, 97% coverage: 28:1046/1054 of query aligns to 17:1016/1023 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 (= D225), H391 (= H421), N460 (= N492), E461 (= E493), Y503 (= Y533), F512 (≠ S535), Q537 (≠ E556), W568 (= W587), W999 (= W1029)
- binding magnesium ion: N18 (≠ T29), V21 (= V32), Q163 (≠ E187), D193 (= D217), D201 (= D225), E416 (= E446), H418 (= H448), E461 (= E493)
Sites not aligning to the query:
7brsA E.Coli beta-galactosidase (e537q) in complex with fluorescent probe ksa02 (see paper)
33% identity, 97% coverage: 28:1046/1054 of query aligns to 15:1014/1021 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 (= D225), E459 (= E493), Y501 (= Y533), Q535 (≠ E556), H538 (= H559), N602 (≠ K628), W997 (= W1029)
- binding magnesium ion: N16 (≠ T29), V19 (= V32), Q161 (≠ E187), D191 (= D217), E414 (= E446), H416 (= H448), E459 (= E493)
Sites not aligning to the query:
6kuzA E.Coli beta-galactosidase (e537q) in complex with fluorescent probe ksl01 (see paper)
33% identity, 97% coverage: 28:1046/1054 of query aligns to 15:1014/1021 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 (= D225), H389 (= H421), H416 (= H448), E459 (= E493), Y501 (= Y533), Q535 (≠ E556), H538 (= H559), W566 (= W587), W997 (= W1029)
- binding magnesium ion: N16 (≠ T29), V19 (= V32), Q161 (≠ E187), D191 (= D217), E414 (= E446), H416 (= H448), E459 (= E493)
Sites not aligning to the query:
1jywA E. Coli (lacz) beta-galactosidase (e537q) in complex with pnpg (see paper)
33% identity, 97% coverage: 28:1046/1054 of query aligns to 5:1004/1011 of 1jywA
- active site: D189 (= D225), H345 (= H387), H379 (= H421), E404 (= E446), H406 (= H448), E449 (= E493), Y491 (= Y533), Q525 (≠ E556), N585 (≠ S621), F589 (= F625), N592 (≠ K628)
- binding 4-nitrophenyl beta-D-galactopyranoside: N90 (= N117), D189 (= D225), E449 (= E493), Y491 (= Y533), Q525 (≠ E556), H528 (= H559), N592 (≠ K628), W987 (= W1029)
- binding magnesium ion: N6 (≠ T29), V9 (= V32), Q151 (≠ E187), D181 (= D217), E404 (= E446), H406 (= H448), E449 (= E493)
Sites not aligning to the query:
1jyvA E. Coli (lacz) beta-galactosidase (e537q) in complex with onpg (see paper)
33% identity, 97% coverage: 28:1046/1054 of query aligns to 5:1004/1011 of 1jyvA
- active site: D189 (= D225), H345 (= H387), H379 (= H421), E404 (= E446), H406 (= H448), E449 (= E493), Y491 (= Y533), Q525 (≠ E556), N585 (≠ S621), F589 (= F625), N592 (≠ K628)
- binding 2-nitrophenyl beta-D-galactopyranoside: N90 (= N117), N90 (= N117), V91 (≠ Q118), D189 (= D225), H406 (= H448), E449 (= E493), Y491 (= Y533), H528 (= H559), D586 (= D622), F589 (= F625), N592 (≠ K628), V783 (≠ A821), V783 (≠ A821), E785 (≠ L823), R788 (≠ K826), W987 (= W1029)
- binding magnesium ion: N6 (≠ T29), V9 (= V32), Q151 (≠ E187), D181 (= D217), E404 (= E446), H406 (= H448), E449 (= E493)
Sites not aligning to the query:
1jynA E. Coli (lacz) beta-galactosidase (e537q) in complex with lactose (see paper)
33% identity, 97% coverage: 28:1046/1054 of query aligns to 5:1004/1011 of 1jynA
- active site: D189 (= D225), H345 (= H387), H379 (= H421), E404 (= E446), H406 (= H448), E449 (= E493), Y491 (= Y533), Q525 (≠ E556), N585 (≠ S621), F589 (= F625), N592 (≠ K628)
- binding beta-D-glucopyranose: N90 (= N117), W987 (= W1029)
- binding beta-D-galactopyranose: N90 (= N117), D189 (= D225), E449 (= E493), Y491 (= Y533), H528 (= H559), N592 (≠ K628), W987 (= W1029)
- binding magnesium ion: N6 (≠ T29), V9 (= V32), Q151 (≠ E187), D181 (= D217), E404 (= E446), H406 (= H448), E449 (= E493)
- binding sodium ion: D189 (= D225), F544 (≠ I575), Y547 (≠ N578), P548 (= P579), L550 (= L581), F589 (= F625), N592 (≠ K628), S635 (≠ I672), D636 (≠ S673), E638 (≠ V675), L658 (= L696), F919 (≠ R948), P920 (= P949), L955 (= L992), M956 (≠ D993), T958 (≠ E995)
Sites not aligning to the query:
4duxA E. Coli (lacz) beta-galactosidase (n460s) in complex with l-ribose (see paper)
33% identity, 97% coverage: 28:1046/1054 of query aligns to 9:1008/1015 of 4duxA
- active site: D193 (= D225), H349 (= H387), H383 (= H421), E408 (= E446), H410 (= H448), E453 (= E493), Y495 (= Y533), E529 (= E556), N589 (≠ S621), F593 (= F625), N596 (≠ K628)
- binding beta-L-ribopyranose: D193 (= D225), H383 (= H421), E453 (= E493), M494 (≠ Q532), Y495 (= Y533), E529 (= E556), H532 (= H559), W560 (= W587), F593 (= F625), S788 (≠ G822), W991 (= W1029)
- binding magnesium ion: N10 (≠ T29), V13 (= V32), Q155 (≠ E187), D185 (= D217), E408 (= E446), H410 (= H448), E453 (= E493)
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: 36:1054/1054 of query aligns to 13:1001/1030 of P06864
- E449 (= E493) active site, Proton donor
1yq2A Beta-galactosidase from arthrobacter sp. C2-2 (isoenzyme c2-2-1) (see paper)
30% identity, 92% coverage: 65:1029/1054 of query aligns to 30:1001/1020 of 1yq2A
- active site: D198 (= D225), H332 (= H387), H366 (= H421), E391 (= E446), H393 (= H448), E439 (= E493), Y480 (= Y533), E518 (= E556), H578 (≠ S621), F582 (= F625), D585 (≠ K628)
- binding magnesium ion: A522 (≠ I560), G524 (= G562), G526 (≠ S564)
3obaA Structure of the beta-galactosidase from kluyveromyces lactis (see paper)
29% identity, 97% coverage: 23:1048/1054 of query aligns to 4:1019/1024 of 3obaA
- active site: D186 (= D225), H354 (= H387), H388 (= H421), E413 (= E446), H415 (= H448), E481 (= E493), Y522 (= Y533), E550 (= E556), H615 (≠ S621), F619 (= F625), D622 (≠ K628)
- binding manganese (iii) ion: D592 (vs. gap), H974 (= H1002), D977 (≠ E1005)
Query Sequence
>CA265_RS04025 FitnessBrowser__Pedo557:CA265_RS04025
MKRKLTILFTSLFIAGQISAQDLPSELQTPEVVSVNRLPMRASAFAFENQDLATKRAKEK
SEYFLSLNGTWKFNWVKDPRKRPTDFYKLDFDDKGWDNFKVPANWETNGYGTPIYVNQPY
EFAGRQLTGARMNPPFDIPADNNPVGSYRKKINIPANWSGRQVFISLGAVKSAFYIWVNG
KKVGYSEDSKLAAEFDITKYVKPGENTIALQVYRWSDGTYLECQDMWRISGIEREVYLYS
TPKLDIRDFKVIGNLDATYTNGLLNVDLAVENYKIDQRTNHSRPDSFYVALDLVDAKGNN
VWKDATTIQKVLGNYKTDLSFKTQISNVKNWSAEIPYLYTLYITLKDKNNKIIEVIPQRV
GFRSVEIKGSDLLVNGKRVFLKGVNRHEHNATQGHTLTHADMEKDMEMMKKLNVNAVRHS
HYPPDPYWMELCDEYGLYVIDEANIESHGRYYSLETTFANDKQWRIPHLERITRMYERDK
NHASVITWSLGNEAGNGVNFYEAYQWLKGKDFRPVQYERAESDFNTDMIVPQYPSPNYLP
RYSKQDKETRPFIMSEYAHIMGNSLGNFKEYWDAIENNPKLQGGFVWEWIDQAIDTVKNG
KRIMAYGGDFPLSGPVDENFSDNDFCVKGVVTAYRGMTPMAVELKKVHQYIKTTFNGNNQ
INVNNSYFFKDISNVQLNWELVEDGKVIENGVVSNLNVGARQTQMLSLPFKTNYAAGKEY
FLNVHYRLKTAEPFLEKGYEVAYEQIALAGTPKANVYNSNKKALKVEQTAEKAVVKGSDF
TITFDLIKGTLASYVSKGQELLASGPQPGFYRAPTDNDIGAGLNTKLRMWRNVYQDNNTS
NIKSTINSTADGFILTVKSSLLKGDAETTQEFNVSADGTVKVNNQFKAVTGNYKSLMRIG
NDLQLKNDYSNIQWYGRGPGENYVDRKTASLIGTYKSTVSDQYFPYARPQESGNKTDVRW
VTFTNKAGKGLRFEFADQLLNFNALPYSVEDLDPEAEKKQYHSGELVKRNQIYVHMDMQQ
LGVQGIDSWGSMPLIQYQIPFKDYQYSYYIKPIK
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