SitesBLAST
Comparing AZOBR_RS08020 FitnessBrowser__azobra:AZOBR_RS08020 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)
7cyxA Crystal strcuture of glycine oxidase from bacillus cereus atcc 14579 (see paper)
25% identity, 95% coverage: 3:415/436 of query aligns to 4:360/363 of 7cyxA
- binding flavin-adenine dinucleotide: I7 (≠ L6), G8 (= G7), G10 (= G9), V11 (= V10), I12 (= I11), V30 (= V29), E31 (≠ D30), K32 (≠ R31), E38 (≠ S52), A39 (= A53), S40 (≠ P54), A43 (= A57), G45 (= G59), L46 (= L60), V171 (≠ I224), G200 (≠ M253), G201 (= G254), W203 (≠ Y256), G298 (= G354), R300 (= R356), P301 (= P357), Y326 (≠ G381), R327 (≠ T382), N328 (≠ L383), G329 (= G384), I330 (≠ W385)
Q5L2C2 Glycine oxidase; GO; GOX; GOXK; EC 1.4.3.19 from Geobacillus kaustophilus (strain HTA426)
29% identity, 68% coverage: 122:416/436 of query aligns to 80:370/377 of Q5L2C2
- V180 (≠ I224) binding
- R309 (= R356) binding
- 334:340 (vs. 380:386, 29% identical) binding
- R336 (≠ T382) binding
Sites not aligning to the query:
- 14:15 binding
- 34:35 binding
- 42:43 binding
- 47:49 binding
4yshB Crystal structure of glycine oxidase from geobacillus kaustophilus
29% identity, 68% coverage: 122:416/436 of query aligns to 79:368/368 of 4yshB
- active site: I262 (≠ V311), L283 (= L332), G305 (= G354), N335 (≠ L383), L338 (≠ T386)
- binding flavin-adenine dinucleotide: V178 (≠ I224), S206 (≠ M253), W209 (≠ Y256), R307 (= R356), H332 (= H380), R334 (≠ T382), N335 (≠ L383), G336 (= G384), I337 (≠ W385), L338 (≠ T386)
- binding glycine: G249 (≠ H298), Y251 (≠ I300), Y251 (≠ I300), A264 (≠ G313), R307 (= R356), R334 (≠ T382), R334 (≠ T382)
Sites not aligning to the query:
- active site: 45, 48, 49, 52
- binding flavin-adenine dinucleotide: 9, 10, 12, 14, 32, 33, 34, 40, 41, 42, 45, 46, 48
4yshA Crystal structure of glycine oxidase from geobacillus kaustophilus
29% identity, 68% coverage: 122:416/436 of query aligns to 79:368/370 of 4yshA
- active site: I262 (≠ V311), L283 (= L332), G305 (= G354), N335 (≠ L383), L338 (≠ T386)
- binding flavin-adenine dinucleotide: V178 (≠ I224), S206 (≠ M253), G207 (= G254), W209 (≠ Y256), R307 (= R356), H332 (= H380), R334 (≠ T382), N335 (≠ L383), G336 (= G384), I337 (≠ W385)
Sites not aligning to the query:
- active site: 45, 48, 49, 52
- binding flavin-adenine dinucleotide: 10, 12, 14, 32, 33, 34, 40, 41, 42, 45, 46, 47, 48
6j39A Crystal structure of cmis2 with inhibitor (see paper)
29% identity, 72% coverage: 92:406/436 of query aligns to 44:359/368 of 6j39A
- binding (3R)-3-[(carboxymethyl)sulfanyl]nonanoic acid: M44 (≠ L92), P46 (≠ A94), N49 (= N97), R243 (≠ S291), Y252 (≠ I300), Y267 (≠ A315), R308 (= R356), R334 (≠ T382), I335 (≠ L383)
- binding flavin-adenine dinucleotide: M44 (≠ L92), A174 (≠ E228), A203 (≠ M253), W206 (≠ Y256), I228 (≠ S277), Y252 (≠ I300), R308 (= R356), S333 (≠ G381), R334 (≠ T382), I335 (≠ L383), G336 (= G384), V337 (≠ W385), Q338 (≠ T386)
Sites not aligning to the query:
- binding flavin-adenine dinucleotide: 7, 9, 10, 11, 29, 30, 31, 32, 36, 37, 38, 40, 41, 42, 43
6j38A Crystal structure of cmis2 (see paper)
29% identity, 72% coverage: 92:406/436 of query aligns to 44:359/368 of 6j38A
- binding flavin-adenine dinucleotide: M44 (≠ L92), A174 (≠ E228), A203 (≠ M253), W206 (≠ Y256), G226 (= G275), G306 (= G354), R308 (= R356), S333 (≠ G381), R334 (≠ T382), I335 (≠ L383), G336 (= G384), V337 (≠ W385), Q338 (≠ T386)
Sites not aligning to the query:
- binding flavin-adenine dinucleotide: 7, 9, 11, 29, 30, 31, 36, 37, 38, 41, 42, 43
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: 1:416/436 of query aligns to 26:400/824 of Q8GAI3
- W66 (= W55) mutation W->F,S: Contains a non-covalently bound FAD. Loss of enzyme activity.
- H67 (≠ A56) mutation to A: Contains a non-covalently bound FAD. Exhibits about 10% of the wild-type enzyme activity.
O31616 Glycine oxidase; GO; EC 1.4.3.19 from Bacillus subtilis (strain 168) (see 3 papers)
28% identity, 54% coverage: 186:421/436 of query aligns to 136:366/369 of O31616
- V174 (≠ I224) binding
- H244 (= H298) 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 (= R356) binding
- 327:333 (vs. 380:386, 29% identical) binding
- R329 (≠ T382) 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.
1ng3A Complex of thio (glycine oxidase) with acetyl-glycine (see paper)
27% identity, 54% coverage: 186:419/436 of query aligns to 136:364/364 of 1ng3A
- binding acetylamino-acetic acid: Y246 (≠ I300), R302 (= R356), R329 (≠ T382)
- binding flavin-adenine dinucleotide: V174 (≠ I224), S202 (≠ M253), G203 (= G254), W205 (≠ Y256), F209 (≠ L260), G300 (= G354), R302 (= R356), H327 (= H380), R329 (≠ T382), N330 (≠ L383), G331 (= G384), I332 (≠ W385)
- binding phosphate ion: R254 (= R308)
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
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)
26% identity, 48% coverage: 206:416/436 of query aligns to 179:389/405 of P40875
- C195 (≠ T222) mutation to S: No change in activity.
- C351 (≠ T378) 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)
27% identity, 44% coverage: 206:399/436 of query aligns to 179:372/405 of Q50LF2
- V197 (≠ I224) binding
- H270 (vs. gap) mutation to A: 10-fold decrease in catalytic efficiency.
- Y272 (≠ K299) mutation to A: 13000-fold decrease in catalytic efficiency.; mutation to F: 130-fold decrease in catalytic efficiency.
- G354 (= G381) binding
- G357 (= G384) binding
- K359 (≠ T386) 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
3ad8B Heterotetrameric sarcosine oxidase from corynebacterium sp. U-96 in complex with pyrrole 2-carboxylate (see paper)
27% identity, 44% coverage: 206:399/436 of query aligns to 178:371/404 of 3ad8B
- active site: G326 (= G354), K358 (≠ T386)
- binding flavin-adenine dinucleotide: V196 (≠ I224), G225 (≠ M253), A226 (≠ G254), H228 (≠ Y256), L247 (= L278), G353 (= G381), T354 (= T382), G355 (≠ L383), G356 (= G384), F357 (≠ W385), K358 (≠ T386)
- binding flavin mononucleotide: V251 (≠ I282), E279 (≠ D307), R322 (≠ E350), W324 (= W352)
- binding pyrrole-2-carboxylate: M264 (≠ D295), Y271 (≠ K299), T354 (= T382), K358 (≠ T386)
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)
27% identity, 44% coverage: 206:399/436 of query aligns to 178:371/404 of 3ad7B
- active site: G326 (= G354), K358 (≠ T386)
- binding flavin-adenine dinucleotide: V196 (≠ I224), G225 (≠ M253), A226 (≠ G254), H228 (≠ Y256), L247 (= L278), G353 (= G381), T354 (= T382), G355 (≠ L383), G356 (= G384), F357 (≠ W385), K358 (≠ T386)
- binding flavin mononucleotide: V251 (≠ I282), K277 (≠ L305), E279 (≠ D307), R322 (≠ E350), W324 (= W352)
- binding [methylthio]acetate: M264 (≠ D295), Y271 (≠ K299), T354 (= T382), K358 (≠ T386)
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
1vrqB Crystal structure of heterotetrameric sarcosine oxidase from corynebacterium sp. U-96 in complex with folinic acid (see paper)
27% identity, 44% coverage: 206:399/436 of query aligns to 178:371/402 of 1vrqB
- active site: G326 (= G354), K358 (≠ T386)
- binding n,n-dimethylglycine: K358 (≠ T386)
- binding flavin-adenine dinucleotide: V196 (≠ I224), A224 (= A252), G225 (≠ M253), H228 (≠ Y256), L247 (= L278), G353 (= G381), T354 (= T382), G355 (≠ L383), G356 (= G384), F357 (≠ W385), K358 (≠ T386)
- binding flavin mononucleotide: V251 (≠ I282), E279 (≠ D307), R322 (≠ E350), W324 (= W352)
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
2gagB Heteroteterameric sarcosine: structure of a diflavin metaloenzyme at 1.85 a resolution (see paper)
27% identity, 45% coverage: 206:403/436 of query aligns to 177:374/403 of 2gagB
- binding flavin-adenine dinucleotide: V195 (≠ I224), G224 (≠ M253), A225 (≠ G254), H227 (≠ Y256), L231 (= L260), L246 (≠ G275), G352 (= G381), T353 (= T382), G354 (≠ L383), G355 (= G384), F356 (≠ W385), K357 (≠ T386)
- binding flavin mononucleotide: V250 (≠ T279), E278 (≠ D307), R321 (≠ E350), W323 (= W352)
- binding 2-furoic acid: M263 (≠ V293), Y270 (≠ K299), K357 (≠ T386)
- binding sulfite ion: K276 (≠ L305)
Sites not aligning to the query:
- active site: 61, 64, 65
- binding flavin-adenine dinucleotide: 26, 28, 29, 30, 51, 52, 58, 59, 60, 62, 63, 64, 66
- binding flavin mononucleotide: 61, 62, 171
- binding 2-furoic acid: 64, 66, 68, 401
- binding sulfite ion: 170
3if9A Crystal structure of glycine oxidase g51s/a54r/h244a mutant in complex with inhibitor glycolate (see paper)
26% identity, 54% coverage: 186:419/436 of query aligns to 136:364/364 of 3if9A
- binding flavin-adenine dinucleotide: P173 (≠ G223), V174 (≠ I224), S202 (≠ M253), G203 (= G254), W205 (≠ Y256), F209 (≠ L260), G300 (= G354), R302 (= R356), H327 (= H380), F328 (≠ G381), R329 (≠ T382), N330 (≠ L383), G331 (= G384), I332 (≠ W385)
- binding glycolic acid: Y246 (≠ I300), R302 (= R356), R329 (≠ T382)
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
S5FMM4 Glycine oxidase; GO; BliGO; EC 1.4.3.19 from Bacillus licheniformis (see paper)
30% identity, 45% coverage: 206:401/436 of query aligns to 156:348/369 of S5FMM4
- S202 (≠ M253) 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 (≠ W385) 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 (≠ V395) 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.
Sites not aligning to the query:
- 51 G→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.
- 54 A→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.
- 81 K→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.
4pabB Crystal structure of the precursor form of rat dmgdh complexed with tetrahydrofolate (see paper)
24% identity, 95% coverage: 4:418/436 of query aligns to 9:390/824 of 4pabB
- active site: T53 (≠ A62), E102 (≠ A149), H226 (≠ G275), Y255 (≠ A301)
- binding flavin-adenine dinucleotide: I11 (≠ L6), G12 (= G7), G14 (= G9), C15 (≠ V10), V16 (≠ I11), L35 (= L37), E36 (= E38), K37 (≠ T39), G43 (= G45), S44 (≠ A53), T45 (≠ P54), H47 (≠ A56), A48 (= A57), A49 (≠ P58), G50 (= G59), L51 (= L60), V175 (≠ I224), A204 (≠ M253), G205 (= G254), W207 (≠ Y256), H226 (≠ G275), Y228 (≠ S277), G326 (= G354), I328 (≠ R356), F353 (≠ H380), Y355 (≠ L383), G356 (= G384), I357 (≠ W385), I358 (≠ T386)
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
Q63342 Dimethylglycine dehydrogenase, mitochondrial; ME2GLYDH; EC 1.5.8.4 from Rattus norvegicus (Rat) (see 2 papers)
24% identity, 95% coverage: 4:418/436 of query aligns to 46:427/857 of Q63342
- CV 52:53 (≠ VI 10:11) binding
- EK 73:74 (≠ ET 38:39) binding
- 80:88 (vs. 45:60, 31% identical) binding
- H84 (≠ A56) modified: Tele-8alpha-FAD histidine
- V212 (≠ I224) binding
- W244 (≠ Y256) binding
- FG-YGII 390:395 (≠ HGTLGWT 380:386) binding
Sites not aligning to the query:
- 573:575 binding
- 669 binding
- 676:678 binding
- 737 binding
1y56B Crystal structure of l-proline dehydrogenase from p.Horikoshii (see paper)
21% identity, 73% coverage: 102:418/436 of query aligns to 53:370/374 of 1y56B
- active site: H224 (≠ G275), P239 (= P289), G305 (= G354), M338 (≠ T386)
- binding flavin-adenine dinucleotide: E170 (≠ G223), V171 (≠ I224), T200 (≠ M253), N201 (≠ G254), W203 (≠ Y256), G305 (= G354), Y306 (≠ L355), Y307 (≠ R356), G334 (≠ T382), H335 (≠ L383), G336 (= G384), F337 (≠ W385), M338 (≠ T386)
- binding flavin mononucleotide: I260 (= I309), R301 (≠ E350), W303 (= W352)
Sites not aligning to the query:
- active site: 44, 47, 48
- binding flavin-adenine dinucleotide: 11, 13, 14, 15, 33, 34, 35, 42, 43, 45, 46, 47, 49
- binding flavin mononucleotide: 44, 45
Query Sequence
>AZOBR_RS08020 FitnessBrowser__azobra:AZOBR_RS08020
MRVIVLGSGVIGVSTAYFLAKAGHEVTVVDRQPGPALETSYANAGEVSPGYSAPWAAPGL
MAKAVKWMLMKHSPLVIRPKMDPAMWSWCLKLLANANERSYEINKGRMVRLAEYSRDCLR
VLRDETGIRYDERAKGTLQVFRTQKQVDAAATDMAVLDRFKVPYSLLDVEGCAAVEPALR
LVKEKIVGGLLLPGDETGDCFRFTNALAAMATELGVEFRYNTGIRKLESDGRRVTGVVTD
AGTLTADSYVVAMGSYSPTLVKPFGLDLPVYPVKGYSLTLPIVDAAGAPESTVMDETHKI
AVTRLGDRIRVGGTAELTGFDLTLRPGRRGPLDHVVSDLFPTGGDLSKAEFWTGLRPNTP
DGTPIVGPTPVRNLFLNTGHGTLGWTMAAGSGRVVADVVGGRQTEIDMDGLTVARYGRSA
AAASRPTVGGVARPAA
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