SitesBLAST
Comparing BPHYT_RS29290 FitnessBrowser__BFirm:BPHYT_RS29290 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 20 (the maximum) hits to proteins with known functional sites (download)
5hxwA L-amino acid deaminase from proteus vulgaris (see paper)
30% identity, 95% coverage: 10:430/441 of query aligns to 9:433/433 of 5hxwA
- active site: F58 (≠ N59), Q61 (≠ W62), A62 (≠ C63), Q240 (≠ I234), V284 (vs. gap), F288 (≠ L284)
- binding cetyl-trimethyl-ammonium: G291 (≠ A287), Y294 (≠ F290), N310 (≠ L306), E311 (= E307), F317 (≠ H313), M318 (≠ E314), S320 (≠ L316), M373 (≠ V369), E379 (≠ G375), G399 (= G396), W400 (≠ H397)
- binding flavin-adenine dinucleotide: V22 (≠ I23), G23 (= G24), G25 (= G26), I26 (= I27), L27 (≠ I28), E46 (= E47), K47 (= K48), E53 (= E54), Q54 (= Q55), S55 (= S56), R57 (= R58), F58 (≠ N59), Y59 (≠ W60), G60 (= G61), Q61 (≠ W62), A188 (= A184), A189 (= A185), G218 (= G214), G219 (= G215), W221 (= W217), Q240 (≠ I234), Q242 (= Q236), F331 (≠ M327), G371 (= G367), M373 (≠ V369), T398 (≠ S395), G399 (= G396), W400 (≠ H397), G401 (= G398), M402 (≠ F399), T403 (≠ G400)
5fjnA Structure of l-amino acid deaminase from proteus myxofaciens in complex with anthranilate (see paper)
31% identity, 95% coverage: 10:430/441 of query aligns to 21:445/447 of 5fjnA
- active site: S67 (= S56), Y71 (≠ W60), S72 (≠ G61), L252 (≠ Q236)
- binding 2-aminobenzoic acid: L252 (≠ Q236), R289 (≠ S272), V411 (≠ G396), W412 (≠ H397)
- binding flavin-adenine dinucleotide: I34 (= I23), G35 (= G24), G37 (= G26), I38 (= I27), Q39 (≠ I28), L57 (≠ V46), E58 (= E47), K59 (= K48), E65 (= E54), Q66 (= Q55), S67 (= S56), A70 (≠ N59), Y71 (≠ W60), S72 (≠ G61), Q73 (≠ W62), V201 (≠ A185), G230 (= G214), G231 (= G215), W233 (= W217), L252 (≠ Q236), Q254 (≠ I238), F343 (≠ M327), V385 (= V369), T410 (≠ S395), V411 (≠ G396), W412 (≠ H397), G413 (= G398), M414 (≠ F399), T415 (≠ G400)
5fjmA Structure of l-amino acid deaminase from proteus myxofaciens (see paper)
31% identity, 95% coverage: 10:430/441 of query aligns to 21:445/447 of 5fjmA
- active site: S67 (= S56), Y71 (≠ W60), S72 (≠ G61), L252 (≠ Q236)
- binding flavin-adenine dinucleotide: I34 (= I23), G35 (= G24), G37 (= G26), I38 (= I27), Q39 (≠ I28), L57 (≠ V46), E58 (= E47), K59 (= K48), E65 (= E54), Q66 (= Q55), S67 (= S56), A70 (≠ N59), Y71 (≠ W60), S72 (≠ G61), Q73 (≠ W62), V201 (≠ A185), G230 (= G214), G231 (= G215), W233 (= W217), L252 (≠ Q236), Q254 (≠ I238), F343 (≠ M327), V385 (= V369), T410 (≠ S395), V411 (≠ G396), W412 (≠ H397), G413 (= G398), M414 (≠ F399), T415 (≠ G400)
5i39A High resolution structure of l-amino acid deaminase from proteus vulgaris with the deletion of the specific insertion sequence (see paper)
29% identity, 95% coverage: 10:430/441 of query aligns to 17:383/383 of 5i39A
- active site: F66 (≠ N59), Q69 (≠ W62), A70 (≠ C63), Q248 (≠ I234), P267 (≠ T254)
- binding flavin-adenine dinucleotide: V30 (≠ I23), G31 (= G24), G33 (= G26), I34 (= I27), L35 (≠ I28), V53 (= V46), E54 (= E47), K55 (= K48), Q62 (= Q55), S63 (= S56), F66 (≠ N59), Y67 (≠ W60), Q69 (≠ W62), A196 (= A184), A197 (= A185), G226 (= G214), G227 (= G215), W229 (= W217), Q248 (≠ I234), Q250 (= Q236), G321 (= G367), M323 (≠ V369), T348 (≠ S395), G349 (= G396), W350 (≠ H397), G351 (= G398), M352 (≠ F399), T353 (≠ G400)
1y56B Crystal structure of l-proline dehydrogenase from p.Horikoshii (see paper)
26% identity, 90% coverage: 33:430/441 of query aligns to 20:368/374 of 1y56B
- active site: F44 (≠ S57), G47 (≠ W60), T48 (≠ G61), H224 (≠ P249), P239 (= P281), G305 (= G367), M338 (≠ G400)
- binding flavin-adenine dinucleotide: I33 (≠ V46), E34 (= E47), K35 (= K48), S42 (≠ Q55), T43 (≠ S56), R45 (= R58), C46 (≠ N59), G47 (≠ W60), G49 (≠ W62), E170 (≠ A184), V171 (≠ A185), T200 (≠ G214), N201 (≠ G215), W203 (= W217), G305 (= G367), Y306 (≠ F368), Y307 (≠ V369), G334 (= G396), H335 (= H397), G336 (= G398), F337 (= F399), M338 (≠ G400)
- binding flavin mononucleotide: F44 (≠ S57), R45 (= R58), I260 (≠ P326), R301 (≠ H363), W303 (= W365)
Sites not aligning to the query:
7cyxA Crystal strcuture of glycine oxidase from bacillus cereus atcc 14579 (see paper)
23% identity, 90% coverage: 19:415/441 of query aligns to 3:346/363 of 7cyxA
- binding flavin-adenine dinucleotide: I7 (= I23), G8 (= G24), G10 (= G26), V11 (≠ I27), I12 (= I28), V30 (= V46), E31 (= E47), K32 (= K48), E38 (= E54), A39 (≠ Q55), S40 (= S56), A43 (≠ N59), G45 (= G61), L46 (≠ W62), V171 (≠ A185), G200 (= G214), G201 (= G215), W203 (= W217), G298 (= G367), R300 (≠ V369), P301 (≠ D370), Y326 (≠ S395), R327 (≠ G396), N328 (≠ H397), G329 (= G398), I330 (≠ F399)
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)
25% identity, 95% coverage: 14:431/441 of query aligns to 22:401/824 of Q8GAI3
- W66 (≠ S57) mutation W->F,S: Contains a non-covalently bound FAD. Loss of enzyme activity.
- H67 (≠ R58) 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)
23% identity, 94% coverage: 18:430/441 of query aligns to 50:432/866 of Q9UI17
- CV 59:60 (≠ II 27:28) binding
- EK 80:81 (= EK 47:48) binding
- 87:95 (vs. 54:62, 11% identical) binding
- H91 (≠ R58) modified: Tele-8alpha-FAD histidine
- H109 (≠ A76) to R: in DMGDHD; shows 10 fold lower catalytic efficiency due to lower cofactor saturation and reduced thermal stability; dbSNP:rs121908331
- V219 (≠ A185) binding
- S279 (≠ L239) to P: in dbSNP:rs532964
- F-GYGII 397:402 (≠ FSGHGFG 394:400) binding
Sites not aligning to the query:
- 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)
24% identity, 97% coverage: 2:430/441 of query aligns to 32:425/857 of Q63342
- CV 52:53 (≠ II 27:28) binding
- EK 73:74 (= EK 47:48) binding
- 80:88 (vs. 54:62, 11% identical) binding
- H84 (≠ R58) modified: Tele-8alpha-FAD histidine
- V212 (≠ A185) binding
- W244 (= W217) binding
- F-GYGII 390:395 (≠ FSGHGFG 394:400) binding
Sites not aligning to the query:
- 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, 94% coverage: 18:430/441 of query aligns to 6:388/824 of 4pabB
- active site: T53 (≠ R64), E102 (≠ R113), H226 (≠ Q236), Y255 (≠ A268)
- binding flavin-adenine dinucleotide: I11 (= I23), G12 (= G24), G14 (= G26), C15 (≠ I27), V16 (≠ I28), L35 (≠ V46), E36 (= E47), K37 (= K48), G43 (≠ E54), S44 (≠ Q55), T45 (≠ S56), H47 (≠ R58), A48 (≠ N59), A49 (≠ W60), G50 (= G61), L51 (≠ W62), V175 (≠ A185), A204 (≠ G214), G205 (= G215), W207 (= W217), H226 (≠ Q236), Y228 (≠ I238), G326 (= G367), I328 (≠ V369), F353 (= F394), Y355 (≠ H397), G356 (= G398), I357 (≠ F399), I358 (≠ G400)
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)
24% identity, 65% coverage: 11:296/441 of query aligns to 13:316/403 of 2gagB
- active site: A61 (≠ S57), T64 (≠ W60), T65 (≠ G61)
- binding flavin-adenine dinucleotide: G26 (= G24), G28 (= G26), G29 (≠ I27), H30 (≠ I28), E51 (= E47), K52 (= K48), G58 (≠ E54), N59 (≠ Q55), M60 (≠ S56), R62 (= R58), N63 (= N59), T64 (≠ W60), I66 (≠ W62), V195 (≠ A185), G224 (= G214), A225 (≠ G215), H227 (≠ W217), L231 (≠ F221), L246 (≠ Q236)
- binding flavin mononucleotide: A61 (≠ S57), R62 (= R58), H171 (≠ P161), V250 (≠ S240), E278 (≠ A268)
- binding 2-furoic acid: T64 (≠ W60), I66 (≠ W62), R68 (= R64), M263 (≠ F253), Y270 (≠ T260)
- binding sulfite ion: K170 (≠ D160), K276 (≠ R266)
Sites not aligning to the query:
3if9A Crystal structure of glycine oxidase g51s/a54r/h244a mutant in complex with inhibitor glycolate (see paper)
22% identity, 86% coverage: 34:412/441 of query aligns to 21:345/364 of 3if9A
- active site: A47 (≠ W60), G48 (= G61), M49 (≠ W62)
- binding flavin-adenine dinucleotide: E34 (= E47), S35 (≠ K48), T42 (≠ Q55), T43 (≠ S56), A46 (≠ N59), A47 (≠ W60), G48 (= G61), M49 (≠ W62), P173 (≠ A184), V174 (≠ A185), S202 (≠ G214), G203 (= G215), W205 (= W217), F209 (= F221), G300 (= G367), R302 (≠ V369), H327 (≠ F394), F328 (≠ S395), R329 (≠ G396), N330 (≠ H397), G331 (= G398), I332 (≠ F399)
- binding glycolic acid: Y246 (≠ S258), R302 (≠ V369), R329 (≠ G396)
Sites not aligning to the query:
O31616 Glycine oxidase; GO; EC 1.4.3.19 from Bacillus subtilis (strain 168) (see 3 papers)
22% identity, 86% coverage: 34:412/441 of query aligns to 21:345/369 of O31616
- ES 34:35 (≠ EK 47:48) binding
- TT 42:43 (≠ QS 55:56) binding
- AGM 47:49 (≠ WGW 60:62) binding
- G51 (vs. gap) 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 (≠ Q66) 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 (≠ A185) binding
- H244 (≠ G256) 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 (≠ V369) binding
- 327:333 (vs. 394:400, 14% identical) binding
- R329 (≠ G396) binding
Sites not aligning to the query:
1ng3A Complex of thio (glycine oxidase) with acetyl-glycine (see paper)
22% identity, 86% coverage: 34:412/441 of query aligns to 21:345/364 of 1ng3A
- active site: A47 (≠ W60), G48 (= G61), M49 (≠ W62)
- binding acetylamino-acetic acid: Y246 (≠ S258), R302 (≠ V369), R329 (≠ G396)
- binding flavin-adenine dinucleotide: F33 (≠ V46), E34 (= E47), S35 (≠ K48), R41 (≠ E54), T42 (≠ Q55), T43 (≠ S56), A46 (≠ N59), A47 (≠ W60), G48 (= G61), M49 (≠ W62), V174 (≠ A185), S202 (≠ G214), G203 (= G215), W205 (= W217), F209 (= F221), G300 (= G367), R302 (≠ V369), H327 (≠ F394), R329 (≠ G396), N330 (≠ H397), G331 (= G398), I332 (≠ F399)
- binding phosphate ion: R89 (≠ G95), R254 (= R266)
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)
24% identity, 60% coverage: 33:296/441 of query aligns to 37:318/405 of P40875
- C146 (vs. gap) mutation to S: No change in activity.
- H173 (≠ P161) 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 (≠ K163) mutation to A: No effect on FMN binding and activity.
- C195 (= C183) mutation to S: 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.
- 351 C→A: No change in activity.
S5FMM4 Glycine oxidase; GO; BliGO; EC 1.4.3.19 from Bacillus licheniformis (see paper)
23% identity, 87% coverage: 33:415/441 of query aligns to 20:348/369 of S5FMM4
- G51 (≠ R64) 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 (≠ N67) 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 (vs. gap) 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 (≠ G214) 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 (≠ F399) 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 (≠ I409) 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.
1pj7A Structure of dimethylglycine oxidase of arthrobacter globiformis in complex with folinic acid (see paper)
26% identity, 51% coverage: 20:244/441 of query aligns to 4:230/827 of 1pj7A
- active site: H222 (≠ Q236)
- binding flavin-adenine dinucleotide: G8 (= G24), G10 (= G26), I11 (= I27), V12 (≠ I28), D32 (≠ E47), Q33 (≠ K48), G41 (vs. gap), S42 (≠ Q55), T43 (≠ S56), H45 (≠ R58), P47 (≠ W60), L49 (≠ W62), T170 (≠ A184), V171 (≠ A185), A200 (≠ G214), G201 (= G215), W203 (= W217), H222 (≠ Q236)
Sites not aligning to the query:
- active site: 256, 549
- binding flavin-adenine dinucleotide: 256, 331, 357, 358, 359, 360
- 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)
26% identity, 51% coverage: 20:244/441 of query aligns to 5:231/828 of 1pj6A
- active site: H223 (≠ Q236)
- binding flavin-adenine dinucleotide: G9 (= G24), G11 (= G26), I12 (= I27), V13 (≠ I28), D33 (≠ E47), Q34 (≠ K48), G42 (vs. gap), S43 (≠ Q55), T44 (≠ S56), H46 (≠ R58), P48 (≠ W60), L50 (≠ W62), V172 (≠ A185), A201 (≠ G214), G202 (= G215), W204 (= W217), H223 (≠ Q236)
Sites not aligning to the query:
3gsiA Crystal structure of d552a dimethylglycine oxidase mutant of arthrobacter globiformis in complex with tetrahydrofolate (see paper)
26% identity, 51% coverage: 20:244/441 of query aligns to 4:230/827 of 3gsiA
- active site: H222 (≠ Q236)
- binding flavin-adenine dinucleotide: G10 (= G26), I11 (= I27), V12 (≠ I28), D32 (≠ E47), Q33 (≠ K48), G41 (vs. gap), S42 (≠ Q55), T43 (≠ S56), H45 (≠ R58), P47 (≠ W60), L49 (≠ W62), T170 (≠ A184), V171 (≠ A185), A200 (≠ G214), G201 (= G215), W203 (= W217), H222 (≠ Q236)
Sites not aligning to the query:
- active site: 256, 549
- binding flavin-adenine dinucleotide: 256, 330, 331, 332, 357, 358, 359, 360
- binding magnesium ion: 254, 409
- binding (6s)-5,6,7,8-tetrahydrofolate: 505, 536, 551, 563, 629, 648, 655, 696
Q9AGP8 Dimethylglycine oxidase; DMGO; EC 1.5.3.10 from Arthrobacter globiformis (see 2 papers)
26% identity, 51% coverage: 20:244/441 of query aligns to 7:233/830 of Q9AGP8
- IV 14:15 (≠ II 27:28) binding
- DQ 35:36 (≠ EK 47:48) binding
- STSH 45:48 (≠ QSSR 55:58) binding
- L52 (≠ W62) binding
- V174 (≠ A185) binding
- H225 (≠ Q236) Important for catalytic activity; mutation to Q: Reduces catalytic efficiency 3-fold and substrate affinity 30-fold.
Sites not aligning to the query:
- 259 Important for catalytic activity; binding ; Y→F: Reduces catalytic efficiency 225-fold and substrate affinity 25-fold.
- 360:363 binding
- 539 binding
- 552 Important for catalytic activity; D→A: No effect on the activity.; D→N: Reduces activity 3-fold.
Query Sequence
>BPHYT_RS29290 FitnessBrowser__BFirm:BPHYT_RS29290
MSPPLTHIQTSPTLPAAADVVVIGGGIIGVFAAYYMAQRGVSVALVEKGRIGAEQSSRNW
GWCRQQNRDERELPIASKSLDLWERFAVESGEDTGFHRCGLLYLSNDDAELARWASWGDF
AKTAGVTTYLLDSKQAAERGKATGRAWKGGVFSPSDGTADPAKAAPAVATALMKLGGSVT
QQCAARGIELEGGRVCGVVTEAGVIKTRTVVLAGGAWASAFCRQLGIRFPQASIRQSILS
VSPVETPLPDALFTSGVSITRRTDGRYALAISGRARVDVTPQFLRFAPQFVPMFAKRWRN
LLPGGLEGVRGGHETLKRWQLDAPTPMERVRILDPKPDMPTVRETHRRAIELLPELGKAK
ITHAWAGFVDSTPDGVPGIGEVPGVPGLILAAGFSGHGFGIGPGAGHLIADLATGAAPIV
DPIPYRPARFADSAWGKVADF
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