SitesBLAST
Comparing Ac3H11_416 FitnessBrowser__acidovorax_3H11:Ac3H11_416 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 4 hits to proteins with known functional sites (download)
1pj7A Structure of dimethylglycine oxidase of arthrobacter globiformis in complex with folinic acid (see paper)
23% identity, 98% coverage: 2:402/410 of query aligns to 3:382/827 of 1pj7A
- active site: H222 (≠ A265), Y256 (≠ S294)
- binding flavin-adenine dinucleotide: G8 (= G7), G10 (= G9), I11 (= I10), V12 (= V11), D32 (≠ E30), Q33 (= Q31), G41 (= G78), S42 (= S92), T43 (≠ A93), H45 (= H95), P47 (vs. gap), L49 (vs. gap), T170 (≠ R217), V171 (≠ I218), A200 (= A246), G201 (= G247), W203 (≠ A249), H222 (≠ A265), Y256 (≠ S294), I331 (≠ A349), V357 (≠ G378), W358 (= W379), V359 (≠ A380), T360 (≠ L381)
Sites not aligning to the query:
- active site: 549
- binding N-[4-({[(6S)-2-amino-5-formyl-4-oxo-3,4,5,6,7,8-hexahydropteridin-6-yl]methyl}amino)benzoyl]-L-glutamic acid: 505, 536, 549, 551, 563, 629, 648, 655, 696
1pj6A Crystal structure of dimethylglycine oxidase of arthrobacter globiformis in complex with folic acid (see paper)
23% identity, 98% coverage: 2:402/410 of query aligns to 4:383/828 of 1pj6A
- active site: H223 (≠ A265), Y257 (≠ S294)
- binding flavin-adenine dinucleotide: G9 (= G7), G11 (= G9), I12 (= I10), V13 (= V11), D33 (≠ E30), Q34 (= Q31), G42 (= G78), S43 (= S92), T44 (≠ A93), H46 (= H95), P48 (vs. gap), L50 (vs. gap), V172 (≠ I218), A201 (= A246), G202 (= G247), W204 (≠ A249), H223 (≠ A265), Y257 (≠ S294), G331 (= G348), I332 (≠ A349), V358 (≠ G378), W359 (= W379), V360 (≠ A380), T361 (≠ L381)
Sites not aligning to the query:
Q9AGP8 Dimethylglycine oxidase; DMGO; EC 1.5.3.10 from Arthrobacter globiformis (see 2 papers)
23% identity, 98% coverage: 2:402/410 of query aligns to 6:385/830 of Q9AGP8
- IV 14:15 (= IV 10:11) binding
- DQ 35:36 (≠ EQ 30:31) binding
- STSH 45:48 (≠ SATH 92:95) binding
- L52 (vs. gap) binding
- V174 (≠ I218) binding
- H225 (≠ A265) Important for catalytic activity; mutation to Q: Reduces catalytic efficiency 3-fold and substrate affinity 30-fold.
- Y259 (≠ S294) Important for catalytic activity; binding ; mutation to F: Reduces catalytic efficiency 225-fold and substrate affinity 25-fold.
- VWVT 360:363 (≠ GWAL 378:381) binding
Sites not aligning to the query:
- 539 binding
- 552 Important for catalytic activity; D→A: No effect on the activity.; D→N: Reduces activity 3-fold.
3gsiA Crystal structure of d552a dimethylglycine oxidase mutant of arthrobacter globiformis in complex with tetrahydrofolate (see paper)
23% identity, 98% coverage: 2:402/410 of query aligns to 3:382/827 of 3gsiA
- active site: H222 (≠ A265), Y256 (≠ S294)
- binding flavin-adenine dinucleotide: G10 (= G9), I11 (= I10), V12 (= V11), D32 (≠ E30), Q33 (= Q31), G41 (= G78), S42 (= S92), T43 (≠ A93), H45 (= H95), P47 (vs. gap), L49 (vs. gap), T170 (≠ R217), V171 (≠ I218), A200 (= A246), G201 (= G247), W203 (≠ A249), H222 (≠ A265), Y256 (≠ S294), G330 (= G348), I331 (≠ A349), F332 (≠ R350), V357 (≠ G378), W358 (= W379), V359 (≠ A380), T360 (≠ L381)
- binding magnesium ion: D254 (≠ Q292)
Sites not aligning to the query:
- active site: 549
- binding magnesium ion: 409
- binding (6s)-5,6,7,8-tetrahydrofolate: 505, 536, 551, 563, 629, 648, 655, 696
Query Sequence
>Ac3H11_416 FitnessBrowser__acidovorax_3H11:Ac3H11_416
MKIAIVGAGIVGVTTAYELASDGHEVTVFEQRSAAAEEASFATAGLLAPHLLTPWAVPGF
GHALRLMGPHATLRLSGGLSRANWAWLSRWRSATHASSAPAAALERLAQYSQSRLQALAQ
RHELDFEASQGRLVLLRTEQERAQLQPALQVLRDSGVALREVDADIARQIEPGLSPEAPL
AGAIHLPDARAGNCRLFAQLLRQGTQGSGVHFAFNTRIDRIGTTPVGVVVQGESDLRRFD
AVVLCAGTASAALLPALGMRLPMAAVYGYSVSAPLRESTHAPQASVVDAAQQISITRLGQ
RVRIAGGAELAGADAEHHAATLQRLYRTLNDWFPGGAQLSSGVQVWRGARPLLPDGAPVV
GASGVPGLWLNTGHGAGGWALACGSARALADLMAQRVPEVPLDGLGMRPF
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