SitesBLAST
Comparing 15852 b1734 cryptic phospho-beta-glucosidase, NAD(P)-binding (NCBI) 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 19 hits to proteins with known functional sites (download)
5c3mB Crystal structure of gan4c, a gh4 6-phospho-glucosidase from geobacillus stearothermophilus
51% identity, 97% coverage: 5:439/450 of query aligns to 1:410/411 of 5c3mB
1up7A Structure of the 6-phospho-beta glucosidase from thermotoga maritima at 2.4 angstrom resolution in the tetragonal form with NAD and glucose-6-phosphate (see paper)
33% identity, 96% coverage: 3:436/450 of query aligns to 1:411/414 of 1up7A
- binding 6-O-phosphono-alpha-D-glucopyranose: R89 (= R96), E105 (= E112), N142 (= N150), N165 (= N173), H194 (= H203), Y240 (= Y258), R260 (= R282), R288 (= R312), G289 (= G313), Y293 (= Y317)
- binding nicotinamide-adenine-dinucleotide: G11 (= G13), S12 (= S14), Y14 (= Y16), D38 (= D40), I39 (≠ V41), K43 (= K45), Q80 (= Q87), F81 (≠ L88), R82 (= R89), E105 (= E112), Y125 (≠ I132), F140 (= F148), N142 (= N150), R288 (= R312), G290 (= G314), Y293 (= Y317)
1up6A Structure of the 6-phospho-beta glucosidase from thermotoga maritima at 2.55 angstrom resolution in the tetragonal form with manganese, NAD+ and glucose-6-phosphate (see paper)
33% identity, 96% coverage: 5:436/450 of query aligns to 2:410/413 of 1up6A
- binding 6-O-phosphono-alpha-D-glucopyranose: R88 (= R96), N164 (= N173), H193 (= H203), Y239 (= Y258), R259 (= R282), G288 (= G313)
- binding manganese (ii) ion: I38 (≠ V41), I38 (≠ V41), D39 (≠ E42), D39 (≠ E42), E40 (≠ G43), C163 (= C172), N164 (= N173), H193 (= H203)
- binding nicotinamide-adenine-dinucleotide: S11 (= S14), Y13 (= Y16), D37 (= D40), I38 (≠ V41), K42 (= K45), Q79 (= Q87), F80 (≠ L88), R81 (= R89), Y124 (≠ I132), F139 (= F148), N141 (= N150), C163 (= C172), N164 (= N173), E267 (= E290)
6dvvA 2.25 angstrom resolution crystal structure of 6-phospho-alpha- glucosidase from klebsiella pneumoniae in complex with NAD and mn2+. (see paper)
28% identity, 97% coverage: 3:439/450 of query aligns to 2:434/435 of 6dvvA
- binding manganese (ii) ion: N147 (= N150), C169 (= C172), H200 (= H203)
- binding nicotinamide-adenine-dinucleotide: G12 (= G13), S13 (= S14), T14 (≠ S15), F15 (≠ Y16), D39 (= D40), N40 (≠ V41), R44 (≠ K45), H84 (≠ Q87), I85 (≠ L88), R86 (= R89), V87 (= V90), E109 (= E112), Y118 (≠ K121), N147 (= N150)
6wbtA 2.52 angstrom resolution crystal structure of 6-phospho-alpha- glucosidase from gut microorganisms in complex with NAD and glucose- 6-phosphate
27% identity, 97% coverage: 3:439/450 of query aligns to 2:441/442 of 6wbtA
- binding 6-O-phosphono-alpha-D-glucopyranose: R93 (= R96), E109 (= E112), N148 (= N150), D171 (≠ N173), M172 (≠ I174), H200 (= H203), W243 (≠ F243), Y265 (= Y258), R285 (≠ K278), R293 (≠ V289)
- binding manganese (ii) ion: N148 (= N150), C170 (= C172), H200 (= H203)
- binding nicotinamide-adenine-dinucleotide: G12 (= G13), S13 (= S14), T14 (≠ S15), Y15 (= Y16), D39 (= D40), I40 (≠ V41), R44 (≠ K47), Q84 (= Q87), M85 (≠ L88), R86 (= R89), Y118 (≠ K121), Y146 (≠ F148), N148 (= N150), C170 (= C172), D171 (≠ N173), H320 (≠ Y317)
Q97LM4 Maltose-6'-phosphate glucosidase MalH; 6-phospho-alpha-glucosidase; 6-phospho-glucosidase; Maltose-6-phosphate hydrolase; EC 3.2.1.122 from Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) (see paper)
26% identity, 97% coverage: 3:439/450 of query aligns to 2:440/441 of Q97LM4
- C169 (= C172) mutation to S: Loss of activity.
- D170 (≠ N173) mutation to N: Loss of activity.
- M171 (≠ I174) mutation to V: Highly reduced activity.
- P172 (= P175) mutation to A: Reduced activity.
1u8xX Crystal structure of glva from bacillus subtilis, a metal-requiring, NAD-dependent 6-phospho-alpha-glucosidase (see paper)
26% identity, 97% coverage: 3:439/450 of query aligns to 2:432/436 of 1u8xX
- binding 6-O-phosphono-alpha-D-glucopyranose: R93 (= R96), E109 (= E112), N147 (= N150), D170 (≠ N173), M171 (≠ I174), H200 (= H203), Y256 (= Y258), R276 (≠ K278)
- binding manganese (ii) ion: C169 (= C172), H200 (= H203)
- binding nicotinamide-adenine-dinucleotide: G10 (= G11), G12 (= G13), S13 (= S14), T14 (≠ S15), F15 (≠ Y16), D39 (= D40), N40 (≠ G43), H84 (≠ Q87), I85 (≠ L88), R86 (= R89), Y90 (≠ L93), E109 (= E112), Y118 (≠ K121), Y145 (≠ F148), N147 (= N150), C169 (= C172), D170 (≠ N173)
P54716 Maltose-6'-phosphate glucosidase; 6-phospho-alpha-D-glucosidase; 6-phosphoryl-O-alpha-D-glucopyranosyl:phosphoglucohydrolase; EC 3.2.1.122 from Bacillus subtilis (strain 168) (see paper)
26% identity, 97% coverage: 3:439/450 of query aligns to 4:441/449 of P54716
- D41 (= D40) mutation D->E,G: Loss of activity.
- E111 (= E112) mutation E->D,G: Loss of activity.
- E359 (= E356) mutation E->D,G: Loss of activity.
6vc6B 2.1 angstrom resolution crystal structure of 6-phospho-alpha- glucosidase from gut microorganisms in complex with NAD and mn2+
27% identity, 97% coverage: 3:437/450 of query aligns to 1:437/440 of 6vc6B
- binding 6-O-phosphono-alpha-D-glucopyranose: R92 (= R96), E108 (= E112), N146 (= N150), D170 (≠ N173), H199 (= H203), W240 (≠ L241), Y262 (= Y258), R282 (≠ K278), R290 (≠ V289)
- binding manganese (ii) ion: C169 (= C172), H199 (= H203)
- binding nicotinamide-adenine-dinucleotide: G11 (= G13), S12 (= S14), T13 (≠ S15), Y14 (= Y16), D38 (= D40), I39 (≠ V41), R43 (≠ K45), M84 (≠ L88), R85 (= R89), D124 (≠ V128), Y144 (≠ F148), N146 (= N150), C169 (= C172), D170 (≠ N173), H318 (≠ A321)
Q9AI65 Alpha-glucosidase; EC 3.2.1.20 from Erwinia rhapontici (Pectobacterium rhapontici) (see paper)
25% identity, 96% coverage: 6:436/450 of query aligns to 4:449/453 of Q9AI65
- E173 (≠ I174) mutation to S: Loss of catalytic activity.
- I174 (≠ P175) mutation to V: No effect on catalytic activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
P39130 Alpha-galacturonidase; EC 3.2.1.67 from Bacillus subtilis (strain 168) (see paper)
24% identity, 95% coverage: 4:429/450 of query aligns to 9:440/446 of P39130
- C172 (≠ V171) mutation to L: Does not significantly affect alpha-galacturonidase activity.
3fefA Crystal structure of putative glucosidase lpld from bacillus subtilis
24% identity, 95% coverage: 4:429/450 of query aligns to 3:434/434 of 3fefA
O33830 Alpha-glucosidase; Maltase; EC 3.2.1.20 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) (see paper)
23% identity, 94% coverage: 5:429/450 of query aligns to 4:465/480 of O33830
- G10 (= G11) mutation to A: Reduced activity. 300-fold reduction of the binding affinity for NAD(+). No change in substrate affinity.
- G12 (= G13) mutation to A: No change in activity and substrate affinity. 5-fold reduction of the binding affinity for NAD(+).
- S13 (= S14) mutation to A: Highly reduced activity. 10-fold reduction of the binding affinity for NAD(+). No change in substrate affinity.
1obbA Alpha-glucosidase a, agla, from thermotoga maritima in complex with maltose and NAD+ (see paper)
23% identity, 94% coverage: 5:429/450 of query aligns to 3:464/478 of 1obbA
- binding alpha-D-glucopyranose: D118 (≠ G118), N152 (= N150), H174 (≠ N173), H202 (= H203), D259 (≠ Y258), R262 (vs. gap), W292 (vs. gap), Y295 (vs. gap)
- binding nicotinamide-adenine-dinucleotide: G9 (= G11), G11 (= G13), M37 (≠ V39), D38 (= D40), I39 (≠ V41), R43 (≠ K47), T83 (≠ Q87), A84 (≠ L88), M85 (≠ R89), H89 (≠ L93), D118 (≠ G118), Y130 (≠ V128), A151 (≠ T149), N152 (= N150), Y295 (vs. gap)
3u95A Crystal structure of a putative alpha-glucosidase from thermotoga neapolitana (see paper)
24% identity, 86% coverage: 5:389/450 of query aligns to 1:407/468 of 3u95A
6kcxA Crystal structure of citrate complex of alpha-glucuronidase (tm0752) from thermotoga maritima (see paper)
22% identity, 82% coverage: 5:374/450 of query aligns to 2:403/470 of 6kcxA
1vjtA Crystal structure of alpha-glucosidase (tm0752) from thermotoga maritima at 2.50 a resolution
22% identity, 82% coverage: 5:374/450 of query aligns to 3:404/471 of 1vjtA
- binding nicotinamide-adenine-dinucleotide: G9 (= G11), G11 (= G13), S12 (= S14), D40 (≠ E42), V41 (≠ G43), H42 (≠ G44), A86 (≠ L88), Y87 (vs. gap), P88 (vs. gap), A161 (≠ T149), N162 (= N150), R312 (≠ Q284)
7ctmA Crystal structure of thermotoga maritima alpha-glucuronidase (tm0752) in complex with nadh and d-glucuronic acid (see paper)
22% identity, 82% coverage: 5:374/450 of query aligns to 2:403/469 of 7ctmA
- binding beta-D-glucopyranuronic acid: R13 (≠ Y16), N161 (= N150), C182 (= C172), H211 (= H203), W246 (≠ F239), D268 (vs. gap), R271 (vs. gap), R300 (≠ M273)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G8 (= G11), G10 (= G13), S11 (= S14), V12 (≠ S15), R13 (≠ Y16), F14 (≠ T17), M38 (≠ V41), D39 (≠ E42), V40 (≠ G43), R44 (≠ K47), T84 (≠ Q87), A85 (≠ L88), Y86 (vs. gap), P87 (vs. gap), L139 (≠ V128), T159 (≠ F148), A160 (≠ T149), N161 (= N150), R311 (≠ Q284)
7br4A Structure of deletion mutant of alpha-glucuronidase (tm0752) from thermotoga maritima (see paper)
22% identity, 82% coverage: 5:374/450 of query aligns to 2:403/468 of 7br4A
- binding manganese (ii) ion: C182 (= C172), H211 (= H203)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G8 (= G11), G10 (= G13), S11 (= S14), D39 (≠ E42), V40 (≠ G43), R44 (≠ K47), T84 (≠ Q87), A85 (≠ L88), Y86 (vs. gap), P87 (vs. gap), L139 (≠ V128), A160 (≠ T149), N161 (= N150), R311 (≠ Q284)
Query Sequence
>15852 b1734 cryptic phospho-beta-glucosidase, NAD(P)-binding (NCBI)
MSQKLKVVTIGGGSSYTPELLEGFIKRYHELPVSELWLVDVEGGKPKLDIIFDLCQRMID
NAGVPMKLYKTLDRREALKDADFVTTQLRVGQLPARELDERIPLSHGYLGQETNGAGGLF
KGLRTIPVIFDIVKDVEELCPNAWVINFTNPAGMVTEAVYRHTGFKRFIGVCNIPIGMKM
FIRDVLMLKDSDDLSIDLFGLNHMVFIKDVLINGKSRFAELLDGVASGQLKASSVKNIFD
LPFSEGLIRSLNLLPCSYLLYYFKQKEMLAIEMGEYYKGGARAQVVQKVEKQLFELYKNP
ELKVKPKELEQRGGAYYSDAACEVINAIYNDKQAEHYVNIPHHGQIDNIPADWAVEMTCK
LGRDGATPHPRITHFDDKVMGLIHTIKGFEIAASNAALSGEFNDVLLALNLSPLVHSDRD
AELLAREMILAHEKWLPNFADCIAELKKAH
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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