SitesBLAST
Comparing H281DRAFT_02167 FitnessBrowser__Burk376:H281DRAFT_02167 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 6 hits to proteins with known functional sites (download)
3dmeA Crystal structure of conserved exported protein from bordetella pertussis. Northeast structural genomics target ber141
65% identity, 98% coverage: 3:361/368 of query aligns to 2:361/366 of 3dmeA
- binding flavin-adenine dinucleotide: I8 (= I9), G9 (= G10), G11 (= G12), V12 (= V13), V13 (= V14), A31 (≠ L32), E32 (= E33), A33 (= A34), T41 (= T42), S42 (= S43), R44 (= R45), N45 (= N46), S46 (= S47), E47 (= E48), V48 (= V49), H50 (= H51), T169 (≠ S170), P170 (= P171), L171 (≠ V172), A202 (≠ S202), A203 (= A203), G204 (= G204), H206 (= H206), L210 (= L210), Y232 (= Y232), P270 (= P270), I313 (= I313), R314 (= R314), I346 (= I346), E347 (= E347), S348 (= S348), P349 (= P349), G350 (= G350), L351 (= L351), T352 (= T352)
Q9UI17 Dimethylglycine dehydrogenase, mitochondrial; ME2GLYDH; EC 1.5.8.4 from Homo sapiens (Human) (see 4 papers)
24% identity, 60% coverage: 2:223/368 of query aligns to 48:267/866 of Q9UI17
- CV 59:60 (≠ VV 13:14) binding
- EK 80:81 (≠ EA 33:34) binding
- 87:95 (vs. 40:46, 11% identical) binding
- H91 (vs. gap) modified: Tele-8alpha-FAD histidine
- H109 (≠ S60) to R: in DMGDHD; shows 10 fold lower catalytic efficiency due to lower cofactor saturation and reduced thermal stability; dbSNP:rs121908331
- V219 (= V172) binding
Sites not aligning to the query:
- 279 S → P: in dbSNP:rs532964
- 397:402 binding
- 530 A → G: in dbSNP:rs1805073
- 646 S → P: in dbSNP:rs1805074
Q63342 Dimethylglycine dehydrogenase, mitochondrial; ME2GLYDH; EC 1.5.8.4 from Rattus norvegicus (Rat) (see 2 papers)
23% identity, 60% coverage: 2:223/368 of query aligns to 41:260/857 of Q63342
- CV 52:53 (≠ VV 13:14) binding
- EK 73:74 (≠ EA 33:34) binding
- 80:88 (vs. 40:46, 11% identical) binding
- H84 (vs. gap) modified: Tele-8alpha-FAD histidine
- V212 (= V172) binding
- W244 (≠ H206) binding
Sites not aligning to the query:
- 390:395 binding
- 573:575 binding
- 669 binding
- 676:678 binding
- 737 binding
4pabB Crystal structure of the precursor form of rat dmgdh complexed with tetrahydrofolate (see paper)
23% identity, 60% coverage: 2:223/368 of query aligns to 4:223/824 of 4pabB
- active site: T53 (≠ E48), E102 (≠ Q101)
- binding flavin-adenine dinucleotide: I11 (= I9), G12 (= G10), G13 (≠ A11), G14 (= G12), C15 (≠ V13), V16 (= V14), L35 (= L32), E36 (= E33), K37 (≠ A34), A42 (≠ G39), G43 (≠ V40), S44 (≠ G41), T45 (= T42), H47 (vs. gap), A48 (≠ S43), A49 (≠ S44), G50 (≠ R45), L51 (≠ N46), P174 (= P171), V175 (= V172), A203 (≠ S202), A204 (= A203), G205 (= G204), F206 (≠ L205), W207 (≠ H206)
Sites not aligning to the query:
- active site: 226, 255, 536
- binding flavin-adenine dinucleotide: 226, 228, 324, 326, 327, 328, 353, 354, 355, 356, 357, 358
- binding (6s)-5,6,7,8-tetrahydrofolate: 493, 523, 536, 538, 550, 612, 613, 630, 632, 639, 641, 680, 700, 701
P40873 Monomeric sarcosine oxidase; MSOX; EC 1.5.3.1 from Arthrobacter sp. (strain TE1826) (see 3 papers)
23% identity, 57% coverage: 5:215/368 of query aligns to 8:216/389 of P40873
- G13 (= G10) mutation to A: Loss of activity.
- A14 (= A11) mutation A->D,K: Loss of activity.; mutation A->I,V: Decrease in activity.; mutation A->L,W,Y: Weak activity.
- G15 (= G12) mutation to A: Loss of activity.
- S16 (≠ V13) mutation to P: Weak activity. Loss of activity; when associated with G-17.
- M17 (≠ V14) mutation to G: Weak activity. Loss of activity; when associated with P-16.
- G18 (= G15) mutation to A: Weak activity.
- D36 (≠ E33) mutation to A: Loss of activity.; mutation to E: Almost no change in activity.; mutation to N: 100-fold decrease in activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 265 mutation C->A,D: Decrease in activity. Stabilizes SoxA against chemicals and metal ions.; mutation C->R,S: Almost no change in activity. Stabilizes SoxA against chemicals and metal ions.
- 318 C→S: Weak activity.
1y56B Crystal structure of l-proline dehydrogenase from p.Horikoshii (see paper)
24% identity, 52% coverage: 19:210/368 of query aligns to 20:207/374 of 1y56B
- active site: F44 (≠ S44), G47 (≠ S47), T48 (≠ E48)
- binding flavin-adenine dinucleotide: I33 (≠ L32), E34 (= E33), K35 (≠ A35), S40 (≠ V40), G41 (= G41), S42 (≠ T42), T43 (≠ S43), R45 (= R45), C46 (≠ N46), G47 (≠ S47), T48 (≠ E48), G49 (≠ V49), E170 (≠ P171), V171 (= V172), A199 (≠ S202), T200 (≠ A203), N201 (≠ G204), W203 (≠ H206), I207 (≠ L210)
- binding flavin mononucleotide: F44 (≠ S44), R45 (= R45), C46 (≠ N46)
Sites not aligning to the query:
- active site: 224, 239, 305, 338
- binding flavin-adenine dinucleotide: 10, 11, 13, 14, 15, 250, 305, 306, 307, 332, 334, 335, 336, 337, 338
- binding flavin mononucleotide: 228, 260, 301, 303
Query Sequence
>H281DRAFT_02167 FitnessBrowser__Burk376:H281DRAFT_02167
MDQIECVVIGAGVVGLAVARALAARGREVIVLEAAEAIGVGTSSRNSEVIHAGIYYPRGS
LKATLCVRGREMLYDYCVEHNVPHSRCGKLLVATSSNQIPQLESIMHKGRENGVLDLMRI
TGDQAQALEPALECVAAVFSPQTGIVDSHQLMLALQGDAERDGAVFAFHSPVEAIEASNG
RFIIKVGGDAPATISSACVINSAGLHANALARKIRGLDARHVPPLYLARGNYFGISGRAP
FSRLIYPMPNEAGLGVHLTIDLGGQARFGPDVEWVDAINYDVDPRRAESFYAAIRAYWPA
LPDNALQPAYAGIRPKLSGPGEPAADFVIQGPAAHGVRGLVNLFGIESPGLTASLAIAQR
VCELSGRA
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