SitesBLAST
Comparing AO356_00055 FitnessBrowser__pseudo5_N2C3_1:AO356_00055 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 16 hits to proteins with known functional sites (download)
Q63342 Dimethylglycine dehydrogenase, mitochondrial; ME2GLYDH; EC 1.5.8.4 from Rattus norvegicus (Rat) (see 2 papers)
24% identity, 89% coverage: 20:406/433 of query aligns to 31:424/857 of Q63342
- CV 52:53 (≠ YT 42:43) binding
- EK 73:74 (≠ EA 62:63) binding
- 80:88 (vs. 69:77, 22% identical) binding
- H84 (≠ R73) modified: Tele-8alpha-FAD histidine
- V212 (= V215) binding
- W244 (≠ Y246) binding
- F-GYGII 390:395 (≠ YNGTGVA 371:377) binding
Sites not aligning to the query:
- 573:575 binding
- 669 binding
- 676:678 binding
- 737 binding
3if9A Crystal structure of glycine oxidase g51s/a54r/h244a mutant in complex with inhibitor glycolate (see paper)
24% identity, 87% coverage: 31:407/433 of query aligns to 3:363/364 of 3if9A
- active site: A47 (≠ G75), G48 (= G76), M49 (≠ V77)
- binding flavin-adenine dinucleotide: G11 (= G39), G13 (= G41), I15 (≠ T43), E34 (= E62), S35 (≠ A63), T42 (≠ A70), T43 (≠ S71), A46 (≠ N74), A47 (≠ G75), G48 (= G76), M49 (≠ V77), P173 (= P214), V174 (= V215), S202 (≠ T243), G203 (≠ N244), W205 (≠ Y246), F209 (≠ T250), G300 (= G346), R302 (≠ V348), H327 (≠ Y371), F328 (≠ N372), R329 (≠ G373), N330 (≠ T374), G331 (= G375), I332 (≠ V376)
- binding glycolic acid: Y246 (= Y287), R302 (≠ V348), R329 (≠ G373)
O31616 Glycine oxidase; GO; EC 1.4.3.19 from Bacillus subtilis (strain 168) (see 3 papers)
22% identity, 83% coverage: 49:407/433 of query aligns to 21:363/369 of O31616
- ES 34:35 (≠ EA 62:63) binding
- TT 42:43 (≠ AS 70:71) binding
- AGM 47:49 (≠ GGV 75:77) binding
- G51 (≠ S79) mutation to R: 130-fold decrease in catalytic efficiency on glycine and 28-fold increase in that on glyphosate.; mutation to S: 60-fold decrease in catalytic efficiency on glycine and 210-fold increase in that on glyphosate; when associated with R-54 and A-244.
- A54 (≠ Y82) mutation to R: 20-fold decrease in catalytic efficiency on glycine and 34-fold increase in that on glyphosate. 60-fold decrease in catalytic efficiency on glycine and 210-fold increase in that on glyphosate; when associated with S-51 and A-244.
- V174 (= V215) binding
- H244 (≠ R285) mutation to A: 2-fold decrease in catalytic efficiency on glycine and similar catalytic efficiency on glyphosate. 60-fold decrease in catalytic efficiency on glycine and 210-fold increase in that on glyphosate; when associated with S-51 and R-54.
- R302 (≠ V348) binding
- 327:333 (vs. 371:377, 14% identical) binding
- R329 (≠ G373) binding
Sites not aligning to the query:
1ng3A Complex of thio (glycine oxidase) with acetyl-glycine (see paper)
23% identity, 87% coverage: 31:407/433 of query aligns to 3:363/364 of 1ng3A
- active site: A47 (≠ G75), G48 (= G76), M49 (≠ V77)
- binding acetylamino-acetic acid: Y246 (= Y287), R302 (≠ V348), R329 (≠ G373)
- binding flavin-adenine dinucleotide: G11 (= G39), G13 (= G41), I15 (≠ T43), F33 (≠ L61), E34 (= E62), S35 (≠ A63), R41 (≠ G69), T42 (≠ A70), T43 (≠ S71), A46 (≠ N74), A47 (≠ G75), G48 (= G76), M49 (≠ V77), V174 (= V215), S202 (≠ T243), G203 (≠ N244), W205 (≠ Y246), F209 (≠ T250), G300 (= G346), R302 (≠ V348), H327 (≠ Y371), R329 (≠ G373), N330 (≠ T374), G331 (= G375), I332 (≠ V376)
- binding phosphate ion: R89 (≠ A124), R254 (= R303)
4pabB Crystal structure of the precursor form of rat dmgdh complexed with tetrahydrofolate (see paper)
24% identity, 87% coverage: 30:406/433 of query aligns to 4:387/824 of 4pabB
- active site: T53 (≠ S79), E102 (vs. gap), H226 (≠ S265), Y255 (≠ W296)
- binding flavin-adenine dinucleotide: I11 (≠ V38), G12 (= G39), G14 (= G41), C15 (≠ Y42), V16 (≠ T43), L35 (= L61), E36 (= E62), K37 (≠ A63), G43 (= G69), S44 (≠ A70), T45 (≠ S71), H47 (≠ R73), A48 (≠ N74), A49 (≠ G75), G50 (= G76), L51 (≠ V77), V175 (= V215), A204 (≠ T243), G205 (≠ N244), W207 (≠ Y246), H226 (≠ S265), Y228 (≠ M267), G326 (= G346), I328 (≠ V348), F353 (≠ Y371), Y355 (≠ T374), G356 (= G375), I357 (≠ V376), I358 (≠ A377)
Sites not aligning to the query:
- active site: 536
- binding (6s)-5,6,7,8-tetrahydrofolate: 523, 536, 538, 550, 612, 613, 632, 639, 680, 700
2gagB Heteroteterameric sarcosine: structure of a diflavin metaloenzyme at 1.85 a resolution (see paper)
27% identity, 80% coverage: 28:375/433 of query aligns to 15:354/403 of 2gagB
- active site: A61 (≠ G72), T64 (≠ G75), T65 (≠ G76)
- binding flavin-adenine dinucleotide: G26 (= G39), G28 (= G41), G29 (≠ Y42), H30 (≠ T43), E51 (= E62), K52 (≠ A63), G58 (= G69), N59 (≠ A70), M60 (≠ S71), R62 (= R73), N63 (= N74), T64 (≠ G75), I66 (≠ V77), V195 (= V215), G224 (≠ T243), A225 (≠ N244), H227 (≠ Y246), L231 (≠ T250), L246 (= L268), G352 (= G373), T353 (= T374), G354 (= G375)
- binding flavin mononucleotide: A61 (≠ G72), R62 (= R73), H171 (≠ P191), V250 (vs. gap), E278 (≠ R295), R321 (≠ H342), W323 (= W344)
- binding 2-furoic acid: T64 (≠ G75), I66 (≠ V77), R68 (≠ S79), M263 (≠ L280), Y270 (= Y287)
- binding sulfite ion: K170 (≠ H190), K276 (≠ M293)
Sites not aligning to the query:
S5FMM4 Glycine oxidase; GO; BliGO; EC 1.4.3.19 from Bacillus licheniformis (see paper)
23% identity, 84% coverage: 31:393/433 of query aligns to 3:349/369 of S5FMM4
- G51 (≠ S79) mutation to S: Shows 4.3- and 107-fold increase of affinity to glyphosate and glycine, respectively. Shows 7.1- and 8-fold increase of affinity and catalytic efficiency to glyphosate, respectively, while the substrate affinity to glycine decreases 235-fold and catalytic efficiency decreases 113-fold; when associated with R-54, R-81, C-202, V-332 and V-342.
- A54 (≠ Y82) mutation to R: Shows 7.1- and 8-fold increase of affinity and catalytic efficiency to glyphosate, respectively, while the substrate affinity to glycine decreases 235-fold and catalytic efficiency decreases 113-fold; when associated with S-51, R-81, C-202, V-332 and V-342.
- K81 (≠ Y119) mutation to R: Shows 7.1- and 8-fold increase of affinity and catalytic efficiency to glyphosate, respectively, while the substrate affinity to glycine decreases 235-fold and catalytic efficiency decreases 113-fold; when associated with S-51, R-54, C-202, V-332 and V-342.
- S202 (≠ T243) mutation to C: Shows 7.1- and 8-fold increase of affinity and catalytic efficiency to glyphosate, respectively, while the substrate affinity to glycine decreases 235-fold and catalytic efficiency decreases 113-fold; when associated with S-51, R-54, R-81, V-332 and V-342.
- I332 (≠ V376) mutation to V: Shows 7.1- and 8-fold increase of affinity and catalytic efficiency to glyphosate, respectively, while the substrate affinity to glycine decreases 235-fold and catalytic efficiency decreases 113-fold; when associated with S-51, R-54, R-81, C-202 and V-342.
- M342 (≠ V386) mutation to V: Shows 7.1- and 8-fold increase of affinity and catalytic efficiency to glyphosate, respectively, while the substrate affinity to glycine decreases 235-fold and catalytic efficiency decreases 113-fold; when associated with S-51, R-54, R-81, C-202 and V-332.
Q9UI17 Dimethylglycine dehydrogenase, mitochondrial; ME2GLYDH; EC 1.5.8.4 from Homo sapiens (Human) (see 4 papers)
23% identity, 87% coverage: 30:406/433 of query aligns to 48:431/866 of Q9UI17
- CV 59:60 (≠ YT 42:43) binding
- EK 80:81 (≠ EA 62:63) binding
- 87:95 (vs. 69:77, 22% identical) binding
- H91 (≠ R73) modified: Tele-8alpha-FAD histidine
- H109 (≠ A90) to R: in DMGDHD; shows 10 fold lower catalytic efficiency due to lower cofactor saturation and reduced thermal stability; dbSNP:rs121908331
- V219 (= V215) binding
- S279 (≠ T274) to P: in dbSNP:rs532964
- F-GYGII 397:402 (≠ YNGTGVA 371:377) binding
Sites not aligning to the query:
- 530 A → G: in dbSNP:rs1805073
- 646 S → P: in dbSNP:rs1805074
7cyxA Crystal strcuture of glycine oxidase from bacillus cereus atcc 14579 (see paper)
24% identity, 84% coverage: 32:394/433 of query aligns to 1:348/363 of 7cyxA
- binding flavin-adenine dinucleotide: I7 (≠ V38), G8 (= G39), G10 (= G41), V11 (≠ Y42), I12 (≠ T43), V30 (≠ L61), E31 (= E62), K32 (≠ A63), E38 (≠ G69), A39 (= A70), S40 (= S71), A43 (≠ N74), G45 (= G76), L46 (≠ V77), V171 (= V215), G200 (≠ T243), G201 (≠ N244), W203 (≠ Y246), G298 (= G346), R300 (≠ V348), P301 (≠ A349), Y326 (≠ N372), R327 (≠ G373), N328 (≠ T374), G329 (= G375), I330 (≠ V376)
1y56B Crystal structure of l-proline dehydrogenase from p.Horikoshii (see paper)
22% identity, 83% coverage: 48:406/433 of query aligns to 20:367/374 of 1y56B
- active site: F44 (≠ G72), G47 (= G75), T48 (≠ G76), H224 (≠ S265), P239 (= P276), G305 (= G346), M338 (≠ A377)
- binding flavin-adenine dinucleotide: I33 (≠ L61), E34 (= E62), K35 (≠ A63), S42 (≠ A70), T43 (≠ S71), R45 (= R73), C46 (≠ N74), G47 (= G75), G49 (≠ V77), E170 (≠ P214), V171 (= V215), T200 (= T243), N201 (= N244), W203 (≠ Y246), G305 (= G346), Y306 (≠ L347), Y307 (≠ V348), G334 (= G373), H335 (≠ T374), G336 (= G375), F337 (≠ V376), M338 (≠ A377)
- binding flavin mononucleotide: F44 (≠ G72), R45 (= R73), I260 (≠ D302), R301 (≠ H342), W303 (= W344)
Sites not aligning to the query:
P40875 Sarcosine oxidase subunit beta; Sarcosine oxidase subunit B; Sarcosine oxidase (5,10-methylenetetrahydrofolate-forming) subunit beta; Tetrameric sarcosine oxidase subunit beta; TSOX subunit beta; EC 1.5.3.24 from Corynebacterium sp. (strain P-1) (see 3 papers)
27% identity, 80% coverage: 28:375/433 of query aligns to 17:356/405 of P40875
- G30 (= G41) mutation to A: Prevents covalent attachment of FMN. Blocks subunit assembly.
- C146 (≠ T172) mutation to S: No change in activity.
- H173 (≠ P191) modified: Tele-8alpha-FMN histidine; mutation to N: Prevents covalent attachment of FMN. Loss of activity. The mutant is considerably less stable than wild-type enzyme, the beta and delta subunits are lost during purification, which yields a stable alpha-gamma complex.
- H175 (≠ N193) mutation to A: No effect on FMN binding and activity.
- C195 (≠ A213) mutation to S: No change in activity.
- C351 (≠ G370) mutation to A: No change in activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1vrqB Crystal structure of heterotetrameric sarcosine oxidase from corynebacterium sp. U-96 in complex with folinic acid (see paper)
26% identity, 80% coverage: 28:375/433 of query aligns to 16:355/402 of 1vrqB
- active site: A62 (≠ G72), T65 (≠ G75), T66 (≠ G76), G326 (= G346)
- binding n,n-dimethylglycine: T65 (≠ G75), I67 (≠ V77), R69 (≠ S79)
- binding flavin-adenine dinucleotide: V26 (= V38), G27 (= G39), G29 (= G41), G30 (≠ Y42), H31 (≠ T43), L51 (= L61), E52 (= E62), K53 (≠ A63), G59 (= G69), N60 (≠ A70), M61 (≠ S71), R63 (= R73), N64 (= N74), T65 (≠ G75), I67 (≠ V77), V196 (= V215), A224 (= A242), G225 (≠ T243), H228 (≠ Y246), L247 (= L268), G353 (= G373), T354 (= T374), G355 (= G375)
- binding flavin mononucleotide: A62 (≠ G72), R63 (= R73), H172 (≠ P191), V251 (vs. gap), E279 (≠ R295), R322 (≠ H342), W324 (= W344)
Sites not aligning to the query:
Q50LF2 Sarcosine oxidase subunit beta; Sarcosine oxidase subunit B; Sarcosine oxidase (5,10-methylenetetrahydrofolate-forming) subunit beta; Tetrameric sarcosine oxidase subunit beta; TSOX subunit beta; EC 1.5.3.24 from Corynebacterium sp. (strain U-96) (see 4 papers)
26% identity, 80% coverage: 28:375/433 of query aligns to 17:356/405 of Q50LF2
- G31 (≠ Y42) binding
- H32 (≠ T43) binding
- E53 (= E62) binding
- N61 (≠ A70) binding
- M62 (≠ S71) binding
- T66 (≠ G75) binding
- I68 (≠ V77) binding
- K172 (≠ H190) mutation to A: Retains 39% of wild-type activity.; mutation to D: Retains 32% of wild-type activity.; mutation to R: Retains 58% of wild-type activity.
- H173 (≠ P191) modified: Tele-8alpha-FMN histidine
- V197 (= V215) binding
- H270 (≠ R285) mutation to A: 10-fold decrease in catalytic efficiency.
- Y272 (= Y287) mutation to A: 13000-fold decrease in catalytic efficiency.; mutation to F: 130-fold decrease in catalytic efficiency.
- G354 (= G373) binding
Sites not aligning to the query:
- 357 binding
- 359 binding ; mutation K->A,D: Loss of activity.; K→R: Retains 0.07% of wild-type activity. Shows higher apparent KM for sarcosine.
3ad8B Heterotetrameric sarcosine oxidase from corynebacterium sp. U-96 in complex with pyrrole 2-carboxylate (see paper)
26% identity, 80% coverage: 28:375/433 of query aligns to 16:355/404 of 3ad8B
- active site: A62 (≠ G72), T65 (≠ G75), T66 (≠ G76), G326 (= G346)
- binding flavin-adenine dinucleotide: V26 (= V38), G27 (= G39), G29 (= G41), G30 (≠ Y42), H31 (≠ T43), E52 (= E62), K53 (≠ A63), G59 (= G69), N60 (≠ A70), M61 (≠ S71), R63 (= R73), N64 (= N74), T65 (≠ G75), I67 (≠ V77), V196 (= V215), G225 (≠ T243), A226 (≠ N244), H228 (≠ Y246), L247 (= L268), G353 (= G373), T354 (= T374), G355 (= G375)
- binding flavin mononucleotide: A62 (≠ G72), R63 (= R73), H172 (≠ P191), V251 (vs. gap), E279 (≠ R295), R322 (≠ H342), W324 (= W344)
- binding pyrrole-2-carboxylate: T65 (≠ G75), I67 (≠ V77), R69 (≠ S79), M264 (≠ L280), Y271 (= Y287), T354 (= T374)
Sites not aligning to the query:
3ad7B Heterotetrameric sarcosine oxidase from corynebacterium sp. U-96 in complex with methylthio acetate (see paper)
26% identity, 80% coverage: 28:375/433 of query aligns to 16:355/404 of 3ad7B
- active site: A62 (≠ G72), T65 (≠ G75), T66 (≠ G76), G326 (= G346)
- binding flavin-adenine dinucleotide: V26 (= V38), G27 (= G39), G29 (= G41), G30 (≠ Y42), H31 (≠ T43), E52 (= E62), K53 (≠ A63), G59 (= G69), N60 (≠ A70), M61 (≠ S71), R63 (= R73), N64 (= N74), T65 (≠ G75), I67 (≠ V77), V196 (= V215), G225 (≠ T243), A226 (≠ N244), H228 (≠ Y246), L247 (= L268), G353 (= G373), T354 (= T374), G355 (= G375)
- binding flavin mononucleotide: A62 (≠ G72), R63 (= R73), H172 (≠ P191), V251 (vs. gap), K277 (≠ M293), E279 (≠ R295), R322 (≠ H342), W324 (= W344)
- binding [methylthio]acetate: I67 (≠ V77), R69 (≠ S79), M264 (≠ L280), Y271 (= Y287), T354 (= T374)
Sites not aligning to the query:
Q8GAI3 4-methylaminobutanoate oxidase (formaldehyde-forming); MABO; Demethylating gamma-N-methylaminobutyrate oxidase; Gamma-N-methylaminobutyrate oxidase 1; EC 1.5.3.19 from Paenarthrobacter nicotinovorans (Arthrobacter nicotinovorans) (see paper)
26% identity, 83% coverage: 35:395/433 of query aligns to 28:388/824 of Q8GAI3
- W66 (≠ G72) mutation W->F,S: Contains a non-covalently bound FAD. Loss of enzyme activity.
- H67 (≠ R73) mutation to A: Contains a non-covalently bound FAD. Exhibits about 10% of the wild-type enzyme activity.
Query Sequence
>AO356_00055 FitnessBrowser__pseudo5_N2C3_1:AO356_00055
MAVSPFAADIASLWQSTAVDAPSFPALEGDRSYDVVVVGGGYTGLSTAHYLAKKGLATVV
LEASRIGWGASGRNGGVVSAKYRISLSKVAARYGLEMAQTMRRLSLESVEHLEELVAVYS
LEAAQYRRSGSLHCAHNEATLDYCVREAQWLHEHLGDSSFEVLCAGQMQEETGSGDFVGG
VLDRGGGLLHPLNFVRGLADGVSAAGVSIHEGAPVMGIRRMGTGVRVETPTGTVRAKQVV
LATNGYSSLTPATAPVRKSVVPFRSAMLATEPLTGPQLELLRHGRSYTETRRMMRWFRMA
EDRLLYGGRGAFGTDDSEAAFNALHEAMVKQFPLLARATITHRWSGLVALTIDSVPHVGR
IDDRVVYAMGYNGTGVAMSSYIGKHVADVIVGRKPELGLMWADKIRRIPFYSLRVPVVRM
VAGWYQFLDAIGR
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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