SitesBLAST
Comparing SM_b21648 FitnessBrowser__Smeli:SM_b21648 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
30% identity, 90% coverage: 4:442/490 of query aligns to 1:410/411 of 5c3mB
Q9AI65 Alpha-glucosidase; EC 3.2.1.20 from Erwinia rhapontici (Pectobacterium rhapontici) (see paper)
28% identity, 89% coverage: 5:439/490 of query aligns to 4:449/453 of Q9AI65
- E173 (≠ G173) mutation to S: Loss of catalytic activity.
- I174 (≠ V174) mutation to V: No effect on catalytic activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
3fefA Crystal structure of putative glucosidase lpld from bacillus subtilis
27% identity, 85% coverage: 1:415/490 of query aligns to 1:419/434 of 3fefA
P39130 Alpha-galacturonidase; EC 3.2.1.67 from Bacillus subtilis (strain 168) (see paper)
27% identity, 85% coverage: 1:415/490 of query aligns to 7:425/446 of P39130
- C172 (≠ L170) mutation to L: Does not significantly affect alpha-galacturonidase activity.
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, 89% coverage: 4:441/490 of query aligns to 4:440/442 of 6wbtA
- binding 6-O-phosphono-alpha-D-glucopyranose: R93 (≠ Y93), E109 (≠ T112), N148 (= N150), D171 (≠ H172), M172 (≠ G173), H200 (= H201), W243 (≠ V246), Y265 (vs. gap), R285 (≠ T283), R293 (≠ T291)
- binding manganese (ii) ion: N148 (= N150), C170 (= C171), H200 (= H201)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), S13 (= S13), T14 (≠ I14), Y15 (≠ F16), D39 (= D39), I40 (≠ L40), R44 (≠ N44), Q84 (≠ C84), M85 (≠ V85), R86 (= R86), Y118 (= Y120), Y146 (= Y148), N148 (= N150), C170 (= C171), D171 (≠ H172), H320 (≠ S318)
O33830 Alpha-glucosidase; Maltase; EC 3.2.1.20 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) (see paper)
24% identity, 88% coverage: 1:432/490 of query aligns to 1:465/480 of O33830
- G10 (= G10) mutation to A: Reduced activity. 300-fold reduction of the binding affinity for NAD(+). No change in substrate affinity.
- G12 (= G12) mutation to A: No change in activity and substrate affinity. 5-fold reduction of the binding affinity for NAD(+).
- S13 (= S13) 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)
24% identity, 88% coverage: 3:432/490 of query aligns to 2:464/478 of 1obbA
- binding alpha-D-glucopyranose: D118 (≠ A115), N152 (= N150), H174 (= H172), H202 (= H201), D259 (≠ H254), R262 (≠ E257), W292 (vs. gap), Y295 (≠ H280)
- binding nicotinamide-adenine-dinucleotide: G9 (= G10), G11 (= G12), M37 (≠ T38), D38 (= D39), I39 (≠ L40), R43 (≠ N44), T83 (≠ C84), A84 (≠ V85), M85 (≠ R86), H89 (≠ E91), D118 (≠ A115), Y130 (≠ V127), A151 (= A149), N152 (= N150), Y295 (≠ H280)
3u95A Crystal structure of a putative alpha-glucosidase from thermotoga neapolitana (see paper)
23% identity, 74% coverage: 4:368/490 of query aligns to 1:392/468 of 3u95A
7ctmA Crystal structure of thermotoga maritima alpha-glucuronidase (tm0752) in complex with nadh and d-glucuronic acid (see paper)
22% identity, 87% coverage: 4:431/490 of query aligns to 2:455/469 of 7ctmA
- binding beta-D-glucopyranuronic acid: R13 (≠ G15), N161 (= N150), C182 (= C171), H211 (= H201), W246 (≠ Y247), D268 (= D277), R271 (≠ H280), R300 (≠ Y301)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G8 (= G10), G10 (= G12), S11 (= S13), V12 (≠ I14), R13 (≠ G15), F14 (= F16), M38 (≠ T38), D39 (= D39), V40 (≠ L40), R44 (≠ N44), T84 (≠ C84), A85 (≠ V85), Y86 (vs. gap), P87 (vs. gap), L139 (≠ V127), T159 (≠ Y148), A160 (= A149), N161 (= N150), R311 (≠ L312)
6kcxA Crystal structure of citrate complex of alpha-glucuronidase (tm0752) from thermotoga maritima (see paper)
22% identity, 87% coverage: 4:431/490 of query aligns to 2:455/470 of 6kcxA
1vjtA Crystal structure of alpha-glucosidase (tm0752) from thermotoga maritima at 2.50 a resolution
22% identity, 87% coverage: 4:431/490 of query aligns to 3:456/471 of 1vjtA
- binding nicotinamide-adenine-dinucleotide: G9 (= G10), G11 (= G12), S12 (= S13), D40 (= D39), V41 (≠ L40), H42 (≠ S41), A86 (≠ V85), Y87 (vs. gap), P88 (vs. gap), A161 (= A149), N162 (= N150), R312 (≠ L312)
7br4A Structure of deletion mutant of alpha-glucuronidase (tm0752) from thermotoga maritima (see paper)
22% identity, 87% coverage: 4:431/490 of query aligns to 2:454/468 of 7br4A
- binding manganese (ii) ion: C182 (= C171), H211 (= H201)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G8 (= G10), G10 (= G12), S11 (= S13), D39 (= D39), V40 (≠ L40), R44 (≠ N44), T84 (≠ C84), A85 (≠ V85), Y86 (vs. gap), P87 (vs. gap), L139 (≠ V127), A160 (= A149), N161 (= N150), R311 (≠ L312)
1u8xX Crystal structure of glva from bacillus subtilis, a metal-requiring, NAD-dependent 6-phospho-alpha-glucosidase (see paper)
26% identity, 80% coverage: 3:396/490 of query aligns to 3:389/436 of 1u8xX
- binding 6-O-phosphono-alpha-D-glucopyranose: R93 (≠ Y93), E109 (≠ T112), N147 (= N150), D170 (≠ H172), M171 (≠ G173), H200 (= H201), Y256 (= Y258), R276 (≠ E282)
- binding manganese (ii) ion: C169 (= C171), H200 (= H201)
- binding nicotinamide-adenine-dinucleotide: G10 (= G10), G12 (= G12), S13 (= S13), T14 (≠ I14), F15 (= F16), D39 (= D39), N40 (≠ L40), H84 (≠ C84), I85 (≠ V85), R86 (= R86), Y90 (≠ L90), E109 (≠ T112), Y118 (= Y120), Y145 (= Y148), N147 (= N150), C169 (= C171), D170 (≠ H172)
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)
24% identity, 89% coverage: 5:439/490 of query aligns to 3:410/413 of 1up6A
- binding 6-O-phosphono-alpha-D-glucopyranose: R88 (≠ Y93), N164 (≠ H172), H193 (= H201), Y239 (= Y286), R259 (vs. gap), G288 (≠ S318)
- binding manganese (ii) ion: I38 (≠ L40), I38 (≠ L40), D39 (≠ S41), D39 (≠ S41), E40 (= E42), C163 (= C171), N164 (≠ H172), H193 (= H201)
- binding nicotinamide-adenine-dinucleotide: S11 (= S13), Y13 (≠ F16), D37 (= D39), I38 (≠ L40), K42 (≠ N44), Q79 (≠ C84), F80 (≠ V85), R81 (= R86), Y124 (≠ F131), F139 (≠ Y148), N141 (= N150), C163 (= C171), N164 (≠ H172), E267 (= E298)
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)
24% identity, 89% coverage: 5:439/490 of query aligns to 4:411/414 of 1up7A
- binding 6-O-phosphono-alpha-D-glucopyranose: R89 (≠ Y93), E105 (≠ D111), N142 (= N150), N165 (≠ H172), H194 (= H201), Y240 (= Y286), R260 (vs. gap), R288 (= R317), G289 (≠ S318), Y293 (vs. gap)
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), S12 (= S13), Y14 (≠ F16), D38 (= D39), I39 (≠ L40), K43 (≠ N44), Q80 (≠ C84), F81 (≠ V85), R82 (= R86), E105 (≠ D111), Y125 (≠ F131), F140 (≠ Y148), N142 (= N150), R288 (= R317), G290 (≠ N319), Y293 (vs. gap)
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)
25% identity, 80% coverage: 3:396/490 of query aligns to 5:398/449 of P54716
- D41 (= D39) mutation D->E,G: Loss of activity.
- E111 (≠ T112) mutation E->D,G: Loss of activity.
- E359 (= E357) mutation E->D,G: Loss of activity.
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)
25% identity, 90% coverage: 1:441/490 of query aligns to 1:439/441 of Q97LM4
- C169 (= C171) mutation to S: Loss of activity.
- D170 (≠ H172) mutation to N: Loss of activity.
- M171 (≠ G173) mutation to V: Highly reduced activity.
- P172 (≠ V174) mutation to A: Reduced activity.
6vc6B 2.1 angstrom resolution crystal structure of 6-phospho-alpha- glucosidase from gut microorganisms in complex with NAD and mn2+
25% identity, 80% coverage: 3:396/490 of query aligns to 2:396/440 of 6vc6B
- binding 6-O-phosphono-alpha-D-glucopyranose: R92 (≠ Y93), E108 (≠ T112), N146 (= N150), D170 (≠ H172), H199 (= H201), W240 (≠ Y258), Y262 (≠ T283), R282 (= R303), R290 (vs. gap)
- binding manganese (ii) ion: C169 (= C171), H199 (= H201)
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), S12 (= S13), T13 (≠ I14), Y14 (vs. gap), D38 (≠ A36), I39 (≠ L37), R43 (≠ S41), M84 (≠ V85), R85 (= R86), D124 (≠ V127), Y144 (= Y148), N146 (= N150), C169 (= C171), D170 (≠ H172), H318 (= H321)
6dvvA 2.25 angstrom resolution crystal structure of 6-phospho-alpha- glucosidase from klebsiella pneumoniae in complex with NAD and mn2+. (see paper)
24% identity, 81% coverage: 1:396/490 of query aligns to 1:391/435 of 6dvvA
- binding manganese (ii) ion: N147 (= N150), C169 (= C171), H200 (= H201)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), S13 (= S13), T14 (≠ I14), F15 (= F16), D39 (≠ L37), N40 (≠ T38), R44 (≠ E42), H84 (≠ C84), I85 (≠ V85), R86 (= R86), V87 (= V87), E109 (≠ T112), Y118 (= Y120), N147 (= N150)
Query Sequence
>SM_b21648 FitnessBrowser__Smeli:SM_b21648
MASFKIAIIGAGSIGFTKKLFTDILSVPELRDVEFALTDLSEHNLAMIKSILDRIVEANE
LPTRVTATTDRRKALEGARYIISCVRVGGLEAYADDIRIPLKYGVDQCVGDTICAGGILY
GQRNIPVILDFCKDIREVAEPGAKFLNYANPMAMNTWAAIEYGKVDTVGLCHGVQHGAEQ
IAEILGARDGELDYICSGINHQTWFVDVRLNGRKVGKDELVAAFEAHPVFSKQEKLRIDV
LKRFGVYSTESNGHLSEYLPWYRKRPDEISRWIDMSDWIHGETGGYLRYSTETRNWFETE
YPRFLEEAGRPLETIRRSNEHASRILEALETGRVYRGHFNVKNNGVITNLPADAIIESPG
FVDRFGINMVAGITLPEACAATCISSVNVQRMSVHAAITGDIDLLKLAVLHDPLVGAICT
PEEVWQMVDEMVVAQAKWLPQYAHAIDAAKERLARATVATREWKGAARREVRSIEEIRAE
KEAAKLRAAG
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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