SitesBLAST
Comparing BPHYT_RS23125 FitnessBrowser__BFirm:BPHYT_RS23125 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
7cyxA Crystal strcuture of glycine oxidase from bacillus cereus atcc 14579 (see paper)
24% identity, 83% coverage: 34:391/430 of query aligns to 3:347/363 of 7cyxA
- binding flavin-adenine dinucleotide: I7 (= I38), G8 (= G39), G10 (= G41), V11 (≠ L42), I12 (≠ T43), V30 (≠ L61), E31 (= E62), K32 (≠ A63), E38 (≠ A69), A39 (= A70), S40 (= S71), A43 (≠ N74), G45 (= G76), L46 (≠ Q77), V171 (= V213), G200 (≠ C241), G201 (≠ N242), W203 (≠ Y244), G298 (= G344), R300 (≠ V346), P301 (≠ D347), Y326 (≠ S370), R327 (≠ G371), N328 (≠ H372), G329 (= G373), I330 (≠ V374)
2gagB Heteroteterameric sarcosine: structure of a diflavin metaloenzyme at 1.85 a resolution (see paper)
25% identity, 83% coverage: 32:388/430 of query aligns to 19:370/403 of 2gagB
- active site: A61 (vs. gap), T64 (≠ G75), T65 (≠ G76)
- binding flavin-adenine dinucleotide: G26 (= G39), G28 (= G41), G29 (≠ L42), H30 (≠ T43), E51 (≠ K65), K52 (≠ V66), G58 (= G72), N59 (vs. gap), M60 (vs. gap), R62 (= R73), N63 (= N74), T64 (≠ G75), I66 (≠ Q77), V195 (= V213), G224 (≠ C241), A225 (≠ N242), H227 (≠ Y244), L231 (= L248), L246 (= L269), G352 (≠ S370), T353 (≠ G371), G354 (≠ H372), G355 (= G373), F356 (≠ V374), K357 (≠ N375)
- binding flavin mononucleotide: A61 (vs. gap), R62 (= R73), H171 (≠ P189), V250 (≠ R273), E278 (≠ R301), R321 (≠ Y340), W323 (= W342)
- binding 2-furoic acid: T64 (≠ G75), I66 (≠ Q77), R68 (≠ I79), M263 (≠ D286), Y270 (= Y293), K357 (≠ N375)
- binding sulfite ion: K170 (≠ H188), K276 (≠ D299)
Sites not aligning to the query:
S5FMM4 Glycine oxidase; GO; BliGO; EC 1.4.3.19 from Bacillus licheniformis (see paper)
24% identity, 80% coverage: 46:391/430 of query aligns to 18:349/369 of S5FMM4
- G51 (≠ I79) 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 (≠ F82) 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 (≠ L109) 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 (≠ C241) 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 (≠ V374) 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 (≠ I384) 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.
5hxwA L-amino acid deaminase from proteus vulgaris (see paper)
28% identity, 49% coverage: 34:244/430 of query aligns to 18:221/433 of 5hxwA
- active site: F58 (≠ N74), Q61 (= Q77), A62 (≠ L78)
- binding flavin-adenine dinucleotide: V22 (≠ I38), G23 (= G39), G25 (= G41), I26 (≠ L42), L27 (≠ T43), E46 (= E62), K47 (≠ A63), E53 (≠ A69), Q54 (≠ A70), S55 (= S71), R57 (= R73), F58 (≠ N74), Y59 (≠ G75), G60 (= G76), Q61 (= Q77), A188 (≠ C212), A189 (≠ V213), G218 (≠ C241), G219 (≠ N242), W221 (≠ Y244)
Sites not aligning to the query:
- active site: 240, 284, 288
- binding cetyl-trimethyl-ammonium: 291, 294, 310, 311, 317, 318, 320, 373, 379, 399, 400
- binding flavin-adenine dinucleotide: 240, 242, 331, 371, 373, 398, 399, 400, 401, 402, 403
5i39A High resolution structure of l-amino acid deaminase from proteus vulgaris with the deletion of the specific insertion sequence (see paper)
28% identity, 49% coverage: 34:244/430 of query aligns to 26:229/383 of 5i39A
- active site: F66 (≠ N74), Q69 (= Q77), A70 (≠ L78)
- binding flavin-adenine dinucleotide: V30 (≠ I38), G31 (= G39), G33 (= G41), I34 (≠ L42), L35 (≠ T43), V53 (≠ L61), E54 (= E62), K55 (≠ A63), Q62 (≠ A70), S63 (= S71), F66 (≠ N74), Y67 (≠ G75), Q69 (= Q77), A196 (≠ C212), A197 (≠ V213), G226 (≠ C241), G227 (≠ N242), W229 (≠ Y244)
Sites not aligning to the query:
- active site: 248, 267
- binding flavin-adenine dinucleotide: 248, 250, 321, 323, 348, 349, 350, 351, 352, 353
5fjnA Structure of l-amino acid deaminase from proteus myxofaciens in complex with anthranilate (see paper)
26% identity, 48% coverage: 47:252/430 of query aligns to 43:245/447 of 5fjnA
- active site: S67 (= S71), Y71 (≠ G75), S72 (≠ G76)
- binding flavin-adenine dinucleotide: L57 (= L61), E58 (= E62), K59 (≠ A63), E65 (≠ A69), Q66 (≠ A70), S67 (= S71), A70 (≠ N74), Y71 (≠ G75), S72 (≠ G76), Q73 (= Q77), V201 (= V213), G230 (vs. gap), G231 (vs. gap), W233 (vs. gap)
Sites not aligning to the query:
- active site: 252
- binding 2-aminobenzoic acid: 252, 289, 411, 412
- binding flavin-adenine dinucleotide: 34, 35, 37, 38, 39, 252, 254, 343, 385, 410, 411, 412, 413, 414, 415
5fjmA Structure of l-amino acid deaminase from proteus myxofaciens (see paper)
26% identity, 48% coverage: 47:252/430 of query aligns to 43:245/447 of 5fjmA
- active site: S67 (= S71), Y71 (≠ G75), S72 (≠ G76)
- binding flavin-adenine dinucleotide: L57 (= L61), E58 (= E62), K59 (≠ A63), E65 (≠ A69), Q66 (≠ A70), S67 (= S71), A70 (≠ N74), Y71 (≠ G75), S72 (≠ G76), Q73 (= Q77), V201 (= V213), G230 (vs. gap), G231 (vs. gap), W233 (vs. gap)
Sites not aligning to the query:
- active site: 252
- binding flavin-adenine dinucleotide: 34, 35, 37, 38, 39, 252, 254, 343, 385, 410, 411, 412, 413, 414, 415
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)
28% identity, 45% coverage: 196:388/430 of query aligns to 180:372/405 of P40875
- C195 (≠ S211) mutation to S: No change in activity.
- C351 (≠ Q367) mutation to A: No change in activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 30 G→A: Prevents covalent attachment of FMN. Blocks subunit assembly.
- 146 C→S: No change in activity.
- 173 modified: Tele-8alpha-FMN histidine; H→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.
- 175 H→A: No effect on FMN binding and activity.
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)
28% identity, 45% coverage: 196:388/430 of query aligns to 180:372/405 of Q50LF2
- V197 (= V213) binding
- H270 (≠ L291) mutation to A: 10-fold decrease in catalytic efficiency.
- Y272 (= Y293) mutation to A: 13000-fold decrease in catalytic efficiency.; mutation to F: 130-fold decrease in catalytic efficiency.
- G354 (≠ S370) binding
- G357 (= G373) binding
- K359 (≠ N375) binding ; mutation K->A,D: Loss of activity.; mutation to R: Retains 0.07% of wild-type activity. Shows higher apparent KM for sarcosine.
Sites not aligning to the query:
- 31 binding
- 32 binding
- 53 binding
- 61 binding
- 62 binding
- 66 binding
- 68 binding
- 172 K→A: Retains 39% of wild-type activity.; K→D: Retains 32% of wild-type activity.; K→R: Retains 58% of wild-type activity.
- 173 modified: Tele-8alpha-FMN histidine
1vrqB Crystal structure of heterotetrameric sarcosine oxidase from corynebacterium sp. U-96 in complex with folinic acid (see paper)
28% identity, 45% coverage: 196:388/430 of query aligns to 179:371/402 of 1vrqB
- active site: G326 (= G344), K358 (≠ N375)
- binding n,n-dimethylglycine: K358 (≠ N375)
- binding flavin-adenine dinucleotide: V196 (= V213), A224 (= A240), G225 (≠ C241), H228 (≠ Y244), L247 (= L269), G353 (≠ S370), T354 (≠ G371), G355 (≠ H372), G356 (= G373), F357 (≠ V374), K358 (≠ N375)
- binding flavin mononucleotide: V251 (≠ R273), E279 (≠ R301), R322 (≠ Y340), W324 (= W342)
Sites not aligning to the query:
- active site: 62, 65, 66
- binding n,n-dimethylglycine: 65, 67, 69, 401
- binding flavin-adenine dinucleotide: 26, 27, 29, 30, 31, 51, 52, 53, 59, 60, 61, 63, 64, 65, 67
- binding flavin mononucleotide: 62, 63, 172
3ad8B Heterotetrameric sarcosine oxidase from corynebacterium sp. U-96 in complex with pyrrole 2-carboxylate (see paper)
28% identity, 45% coverage: 196:388/430 of query aligns to 179:371/404 of 3ad8B
- active site: G326 (= G344), K358 (≠ N375)
- binding flavin-adenine dinucleotide: V196 (= V213), G225 (≠ C241), A226 (≠ N242), H228 (≠ Y244), L247 (= L269), G353 (≠ S370), T354 (≠ G371), G355 (≠ H372), G356 (= G373), F357 (≠ V374), K358 (≠ N375)
- binding flavin mononucleotide: V251 (≠ R273), E279 (≠ R301), R322 (≠ Y340), W324 (= W342)
- binding pyrrole-2-carboxylate: M264 (≠ D286), Y271 (= Y293), T354 (≠ G371), K358 (≠ N375)
Sites not aligning to the query:
- active site: 62, 65, 66
- binding flavin-adenine dinucleotide: 26, 27, 29, 30, 31, 52, 53, 59, 60, 61, 63, 64, 65, 67
- binding flavin mononucleotide: 62, 63, 172
- binding pyrrole-2-carboxylate: 65, 67, 69, 402
3ad7B Heterotetrameric sarcosine oxidase from corynebacterium sp. U-96 in complex with methylthio acetate (see paper)
28% identity, 45% coverage: 196:388/430 of query aligns to 179:371/404 of 3ad7B
- active site: G326 (= G344), K358 (≠ N375)
- binding flavin-adenine dinucleotide: V196 (= V213), G225 (≠ C241), A226 (≠ N242), H228 (≠ Y244), L247 (= L269), G353 (≠ S370), T354 (≠ G371), G355 (≠ H372), G356 (= G373), F357 (≠ V374), K358 (≠ N375)
- binding flavin mononucleotide: V251 (≠ R273), K277 (≠ D299), E279 (≠ R301), R322 (≠ Y340), W324 (= W342)
- binding [methylthio]acetate: M264 (≠ D286), Y271 (= Y293), T354 (≠ G371), K358 (≠ N375)
Sites not aligning to the query:
- active site: 62, 65, 66
- binding flavin-adenine dinucleotide: 26, 27, 29, 30, 31, 52, 53, 59, 60, 61, 63, 64, 65, 67
- binding flavin mononucleotide: 62, 63, 172
- binding [methylthio]acetate: 67, 69, 402
Q63342 Dimethylglycine dehydrogenase, mitochondrial; ME2GLYDH; EC 1.5.8.4 from Rattus norvegicus (Rat) (see 2 papers)
22% identity, 56% coverage: 34:274/430 of query aligns to 44:276/857 of Q63342
- CV 52:53 (≠ LT 42:43) binding
- EK 73:74 (≠ EA 62:63) binding
- 80:88 (vs. 68:86, 14% identical) binding
- H84 (≠ A69) modified: Tele-8alpha-FAD histidine
- V212 (= V213) binding
- W244 (≠ Y244) 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)
22% identity, 56% coverage: 34:274/430 of query aligns to 7:239/824 of 4pabB
- active site: T53 (= T88), E102 (≠ A141), H226 (≠ T261)
- binding flavin-adenine dinucleotide: I11 (= I38), G12 (= G39), G14 (= G41), C15 (≠ L42), V16 (≠ T43), L35 (= L61), E36 (= E62), K37 (≠ A63), G43 (vs. gap), S44 (vs. gap), T45 (vs. gap), H47 (≠ A69), A48 (= A70), A49 (≠ S71), G50 (= G72), L51 (≠ I86), V175 (= V213), A204 (≠ C241), G205 (≠ N242), W207 (≠ Y244), H226 (≠ T261), Y228 (≠ V263)
Sites not aligning to the query:
- active site: 255, 536
- binding flavin-adenine dinucleotide: 326, 328, 353, 355, 356, 357, 358
- binding (6s)-5,6,7,8-tetrahydrofolate: 523, 536, 538, 550, 612, 613, 632, 639, 680, 700
1y56B Crystal structure of l-proline dehydrogenase from p.Horikoshii (see paper)
20% identity, 79% coverage: 48:388/430 of query aligns to 20:351/374 of 1y56B
- active site: F44 (≠ G72), G47 (= G75), T48 (≠ G76), H224 (≠ A274), P239 (≠ S287), G305 (= G344), M338 (≠ N375)
- binding flavin-adenine dinucleotide: I33 (≠ L61), E34 (= E62), K35 (≠ A63), S42 (≠ A70), T43 (≠ S71), R45 (= R73), C46 (≠ N74), G47 (= G75), G49 (≠ Q77), E170 (≠ C212), V171 (= V213), T200 (≠ C241), N201 (= N242), W203 (≠ Y244), G305 (= G344), Y306 (≠ F345), Y307 (≠ V346), G334 (= G371), H335 (= H372), G336 (= G373), F337 (≠ V374), M338 (≠ N375)
- binding flavin mononucleotide: F44 (≠ G72), R45 (= R73), I260 (≠ D299), R301 (≠ Y340), W303 (= W342)
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)
27% identity, 60% coverage: 1:256/430 of query aligns to 1:239/824 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.
Q9UI17 Dimethylglycine dehydrogenase, mitochondrial; ME2GLYDH; EC 1.5.8.4 from Homo sapiens (Human) (see 4 papers)
22% identity, 56% coverage: 34:274/430 of query aligns to 51:283/866 of Q9UI17
- CV 59:60 (≠ LT 42:43) binding
- EK 80:81 (≠ EA 62:63) binding
- 87:95 (vs. 68:86, 14% identical) binding
- H91 (≠ A69) modified: Tele-8alpha-FAD histidine
- H109 (≠ W102) to R: in DMGDHD; shows 10 fold lower catalytic efficiency due to lower cofactor saturation and reduced thermal stability; dbSNP:rs121908331
- V219 (= V213) binding
- S279 (≠ D270) to P: in dbSNP:rs532964
Sites not aligning to the query:
- 397:402 binding
- 530 A → G: in dbSNP:rs1805073
- 646 S → P: in dbSNP:rs1805074
3if9A Crystal structure of glycine oxidase g51s/a54r/h244a mutant in complex with inhibitor glycolate (see paper)
22% identity, 53% coverage: 176:402/430 of query aligns to 137:360/364 of 3if9A
- binding flavin-adenine dinucleotide: P173 (≠ C212), V174 (= V213), S202 (≠ C241), G203 (≠ N242), W205 (≠ Y244), F209 (≠ L248), G300 (= G344), R302 (≠ V346), H327 (≠ F369), F328 (≠ S370), R329 (≠ G371), N330 (≠ H372), G331 (= G373), I332 (≠ V374)
- binding glycolic acid: Y246 (= Y293), R302 (≠ V346), R329 (≠ G371)
Sites not aligning to the query:
- active site: 47, 48, 49
- binding flavin-adenine dinucleotide: 11, 13, 15, 34, 35, 42, 43, 46, 47, 48, 49
1ng3A Complex of thio (glycine oxidase) with acetyl-glycine (see paper)
22% identity, 53% coverage: 176:402/430 of query aligns to 137:360/364 of 1ng3A
- binding acetylamino-acetic acid: Y246 (= Y293), R302 (≠ V346), R329 (≠ G371)
- binding flavin-adenine dinucleotide: V174 (= V213), S202 (≠ C241), G203 (≠ N242), W205 (≠ Y244), F209 (≠ L248), G300 (= G344), R302 (≠ V346), H327 (≠ F369), R329 (≠ G371), N330 (≠ H372), G331 (= G373), I332 (≠ V374)
- binding phosphate ion: R254 (= R301)
Sites not aligning to the query:
- active site: 47, 48, 49
- binding flavin-adenine dinucleotide: 11, 13, 15, 33, 34, 35, 41, 42, 43, 46, 47, 48, 49
- binding phosphate ion: 89
O31616 Glycine oxidase; GO; EC 1.4.3.19 from Bacillus subtilis (strain 168) (see 3 papers)
22% identity, 53% coverage: 176:402/430 of query aligns to 137:360/369 of O31616
- V174 (= V213) binding
- H244 (≠ K281) 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 (≠ V346) binding
- 327:333 (vs. 369:375, 14% identical) binding
- R329 (≠ G371) binding
Sites not aligning to the query:
- 14:15 binding
- 34:35 binding
- 42:43 binding
- 47:49 binding
- 51 G→R: 130-fold decrease in catalytic efficiency on glycine and 28-fold increase in that on glyphosate.; G→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.
- 54 A→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.
Query Sequence
>BPHYT_RS23125 FitnessBrowser__BFirm:BPHYT_RS23125
MLRFSNQPHVASYYAATANDSTRHPALDETISVDVCVIGAGLTGISTALNLAERGHSVAV
LEASKVGWAASGRNGGQLIGGFACDIDTFAKYLPADDVKRVWDMGIETLDIVKERVAKHQ
IDCDLTIGYLTAANKPRDTDALQKWRDEAQRRFGYDRLSYVDADGVGNYVQSQRYLGGLF
DADSGHLHPLNYTLGLARAAREAGVQIFEDSCVTALREEDGRHVAETARGRVQARFVVLA
CNTYLGQLAPDVANKIMPVGTYVIATEPLDPDRAEALMPAKAAVCDSRFVLDYFRPAPDH
RLLWGGKVSYSKLAPRNLGEAMRRDMLKTFPQLDDVKIDYAWGGFVDITMNRAPHFGRLS
PTVYFAQGFSGHGVNTTGLAGKLIAEAIDGQASRFDLFGKIRHRDFPGGATLRTPALVLA
MAWYRMKDLI
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