SitesBLAST
Comparing BPHYT_RS20755 FitnessBrowser__BFirm:BPHYT_RS20755 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)
4a35A Crystal structure of human mitochondrial enolase superfamily member 1 (enosf1) (see paper)
62% identity, 99% coverage: 4:431/432 of query aligns to 7:436/441 of 4a35A
- active site: K221 (= K218), K223 (= K220), D251 (= D248), N253 (= N250), E277 (= E274), E306 (= E301), D329 (= D324), H356 (= H351), S380 (= S375), E387 (= E382)
- binding magnesium ion: Y188 (= Y185), D251 (= D248), E277 (= E274), E306 (= E301), Y374 (= Y369)
Q7L5Y1 Mitochondrial enolase superfamily member 1; Antisense RNA to thymidylate synthase; rTS; L-fuconate dehydratase; EC 4.2.1.68 from Homo sapiens (Human) (see 5 papers)
62% identity, 99% coverage: 4:431/432 of query aligns to 6:435/443 of Q7L5Y1
- M145 (≠ E143) to T: in dbSNP:rs2612086
- S148 (≠ R146) modified: Phosphoserine
- D250 (= D248) binding
- E276 (= E274) binding
- E305 (= E301) binding
Sites not aligning to the query:
- 1:27 mutation Missing: Impairs protein solubility. Abolishes catalytic activity.
4ip5A Crystal structure of l-fuconate dehydratase from silicibacter sp. Tm1040 liganded with mg and d-erythronohydroxamate
60% identity, 97% coverage: 4:424/432 of query aligns to 3:421/421 of 4ip5A
- active site: K217 (= K220), D245 (= D248), N247 (= N250), E271 (= E274), E298 (= E301), D321 (= D324), H348 (= H351), E379 (= E382)
- binding (2r,3r)-n,2,3,4-tetrahydroxybutanamide: G21 (= G22), D23 (= D24), Y31 (= Y32), K215 (= K218), K217 (= K220), D245 (= D248), N247 (= N250), E298 (= E301), H348 (= H351)
- binding magnesium ion: D245 (= D248), E271 (= E274), E298 (= E301)
4ip4A Crystal structure of l-fuconate dehydratase from silicibacter sp. Tm1040 liganded with mg
60% identity, 97% coverage: 4:424/432 of query aligns to 3:421/421 of 4ip4A
Q8P3K2 L-fuconate dehydratase; FucD; EC 4.2.1.68 from Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25) (see paper)
56% identity, 100% coverage: 1:430/432 of query aligns to 1:430/441 of Q8P3K2
- GSD 22:24 (= GSD 22:24) binding
- Y32 (= Y32) binding
- K218 (= K218) binding
- K220 (= K220) mutation to A: Inactive.
- D248 (= D248) binding
- N250 (= N250) binding
- E274 (= E274) binding ; binding
- E301 (= E301) binding ; binding
- HAG 351:353 (= HAG 351:353) binding
- E382 (= E382) binding
1yeyC Crystal structure of l-fuconate dehydratase from xanthomonas campestris pv. Campestris str. Atcc 33913
56% identity, 100% coverage: 1:430/432 of query aligns to 1:430/435 of 1yeyC
- active site: T55 (= T55), T190 (= T190), K218 (= K218), K220 (= K220), D248 (= D248), N250 (= N250), E274 (= E274), G300 (= G300), E301 (= E301), D324 (= D324), P350 (= P350), H351 (= H351), A352 (= A352), D368 (= D368), K375 (≠ S375), E382 (= E382)
- binding magnesium ion: D248 (= D248), E274 (= E274), E301 (= E301)
2hxtA Crystal structure of l-fuconate dehydratase from xanthomonas campestris liganded with mg++ and d-erythronohydroxamate (see paper)
56% identity, 99% coverage: 3:430/432 of query aligns to 2:429/434 of 2hxtA
- active site: T54 (= T55), T189 (= T190), K217 (= K218), K219 (= K220), D247 (= D248), N249 (= N250), E273 (= E274), G299 (= G300), E300 (= E301), D323 (= D324), P349 (= P350), H350 (= H351), A351 (= A352), D367 (= D368), K374 (≠ S375), E381 (= E382)
- binding (2r,3r)-n,2,3,4-tetrahydroxybutanamide: G21 (= G22), D23 (= D24), Y31 (= Y32), K217 (= K218), K219 (= K220), E300 (= E301), H350 (= H351), G352 (= G353), E381 (= E382)
- binding magnesium ion: D247 (= D248), E273 (= E274), E300 (= E301)
2hxuA Crystal structure of k220a mutant of l-fuconate dehydratase from xanthomonas campestris liganded with mg++ and l-fuconate (see paper)
56% identity, 99% coverage: 3:430/432 of query aligns to 2:429/434 of 2hxuA
- active site: T54 (= T55), T189 (= T190), K217 (= K218), A219 (≠ K220), D247 (= D248), N249 (= N250), E273 (= E274), G299 (= G300), E300 (= E301), D323 (= D324), P349 (= P350), H350 (= H351), A351 (= A352), D367 (= D368), K374 (≠ S375), E381 (= E382)
- binding 6-deoxy-L-galactonic acid: G21 (= G22), D23 (= D24), Y31 (= Y32), W193 (= W194), K217 (= K218), D247 (= D248), E300 (= E301), H350 (= H351), G352 (= G353), E381 (= E382)
- binding magnesium ion: D247 (= D248), E273 (= E274), E300 (= E301)
4h19A Crystal structure of an enolase (mandelate racemase subgroup, target efi-502087) from agrobacterium tumefaciens, with bound mg and d- ribonohydroxamate, ordered loop
29% identity, 88% coverage: 43:422/432 of query aligns to 39:367/372 of 4h19A
- active site: T51 (= T55), T143 (= T190), K172 (= K218), K174 (= K220), D203 (= D248), N205 (= N250), E229 (= E274), G254 (= G300), E255 (= E301), Q276 (= Q322), D278 (= D324), H305 (= H351), A306 (= A352), G307 (= G353), E327 (= E382)
- binding (2R,3R,4R)-N,2,3,4,5-pentakis(oxidanyl)pentanamide: H52 (vs. gap), K172 (= K218), K174 (= K220), D203 (= D248), N205 (= N250), E229 (= E274), E255 (= E301), H305 (= H351), E327 (= E382)
- binding calcium ion: D268 (≠ Q314), H298 (≠ F344)
- binding magnesium ion: D203 (= D248), E229 (= E274), E255 (= E301)
Sites not aligning to the query:
Q8ZL58 L-talarate/galactarate dehydratase; TalrD/GalrD; StTGD; EC 4.2.1.156; EC 4.2.1.42 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
27% identity, 89% coverage: 30:414/432 of query aligns to 56:380/398 of Q8ZL58
- KR 82:83 (≠ IG 56:57) binding
- K195 (= K218) binding
- K197 (= K220) active site, Proton acceptor; mutation to A: Loss of dehydration activity on both L-talarate and galactarate and loss of epimerization activity.
- D226 (= D248) binding
- N228 (= N250) binding
- E252 (= E274) binding
- E278 (= E301) binding
- H328 (= H351) active site, Proton donor/acceptor; mutation H->N,A: Loss of dehydration activity on both L-talarate and galactarate and loss of epimerization activity.
- E348 (= E382) binding
Sites not aligning to the query:
2pp1A Crystal structure of l-talarate/galactarate dehydratase from salmonella typhimurium lt2 liganded with mg and l-lyxarohydroxamate (see paper)
27% identity, 89% coverage: 30:414/432 of query aligns to 53:377/395 of 2pp1A
- active site: S78 (≠ T55), K192 (= K218), K194 (= K220), D223 (= D248), N225 (= N250), E249 (= E274), G274 (= G300), E275 (= E301), D298 (= D324), H325 (= H351), E345 (= E382)
- binding (2r,3s,4r)-2,3,4-trihydroxy-5-(hydroxyamino)-5-oxopentanoic acid: K79 (≠ I56), F168 (≠ W194), K194 (= K220), E275 (= E301), H325 (= H351), E345 (= E382)
- binding magnesium ion: D223 (= D248), E249 (= E274), E275 (= E301)
Sites not aligning to the query:
2pp3A Crystal structure of l-talarate/galactarate dehydratase mutant k197a liganded with mg and l-glucarate (see paper)
27% identity, 89% coverage: 30:414/432 of query aligns to 53:377/395 of 2pp3A
- active site: S78 (≠ T55), K192 (= K218), A194 (≠ K220), D223 (= D248), N225 (= N250), E249 (= E274), G274 (= G300), E275 (= E301), D298 (= D324), H325 (= H351), E345 (= E382)
- binding l-glucaric acid: K79 (≠ I56), K192 (= K218), D223 (= D248), N225 (= N250), E275 (= E301), H325 (= H351), E345 (= E382), F347 (≠ V384)
- binding magnesium ion: D223 (= D248), E249 (= E274), E275 (= E301)
Sites not aligning to the query:
4hpnA Crystal structure of a proposed galactarolactone cycloisomerase from agrobacterium tumefaciens, target efi-500704, with bound ca, ordered loops (see paper)
32% identity, 50% coverage: 211:426/432 of query aligns to 157:377/378 of 4hpnA
- active site: K164 (= K218), K166 (= K220), D194 (= D248), N196 (= N250), E220 (= E274), G245 (= G300), E246 (= E301), T247 (≠ H302), Q267 (= Q322), D269 (= D324), H296 (= H351), V297 (≠ A352), W298 (≠ G353), R320 (≠ S373), E329 (= E382), F330 (≠ Y383), H334 (= H388)
- binding calcium ion: D194 (= D248), D209 (≠ R263), E220 (= E274), G237 (≠ R291), E246 (= E301)
Sites not aligning to the query:
3ozmA Crystal structure of enolase superfamily member from bordetella bronchiseptica complexed with mg, m-xylarate and l-lyxarate
27% identity, 84% coverage: 68:432/432 of query aligns to 66:376/386 of 3ozmA
- active site: S143 (≠ F150), K170 (= K218), K172 (= K220), D200 (= D248), N202 (= N250), E226 (= E274), G252 (= G300), E253 (= E301), N254 (≠ H302), Q274 (= Q322), D276 (= D324), H303 (= H351), T304 (vs. gap), F305 (vs. gap), E328 (≠ D368), I331 (≠ C371), H333 (≠ S373)
- binding D-xylaric acid: Y146 (≠ V153), K170 (= K218), K172 (= K220), D200 (= D248), N202 (= N250), E253 (= E301), H303 (= H351), F305 (vs. gap), E328 (≠ D368)
- binding magnesium ion: D200 (= D248), E226 (= E274), E253 (= E301)
Sites not aligning to the query:
3ozmD Crystal structure of enolase superfamily member from bordetella bronchiseptica complexed with mg, m-xylarate and l-lyxarate
27% identity, 84% coverage: 68:432/432 of query aligns to 66:376/381 of 3ozmD
- active site: S143 (≠ F150), K170 (= K218), K172 (= K220), D200 (= D248), N202 (= N250), E226 (= E274), G252 (= G300), E253 (= E301), N254 (≠ H302), Q274 (= Q322), D276 (= D324), H303 (= H351), T304 (vs. gap), F305 (vs. gap), E328 (≠ D368), I331 (≠ C371), H333 (≠ S373)
- binding L-arabinaric acid: K172 (= K220), D200 (= D248), N202 (= N250), E253 (= E301), H303 (= H351), F305 (vs. gap), E328 (≠ D368)
- binding magnesium ion: D200 (= D248), E226 (= E274), E253 (= E301)
Sites not aligning to the query:
3op2A Crystal structure of putative mandelate racemase from bordetella bronchiseptica rb50 complexed with 2-oxoglutarate/phosphate
30% identity, 58% coverage: 183:432/432 of query aligns to 131:371/375 of 3op2A
- active site: S138 (≠ T190), K165 (= K218), K167 (= K220), D195 (= D248), N197 (= N250), E221 (= E274), G247 (= G300), E248 (= E301), N249 (≠ H302), Q269 (= Q322), D271 (= D324), H298 (= H351), T299 (vs. gap), F300 (vs. gap), E323 (≠ D368), I326 (≠ C371), H328 (≠ S373)
- binding 2-oxoglutaric acid: K165 (= K218), K167 (= K220), D195 (= D248), E248 (= E301), H298 (= H351), E323 (≠ D368)
- binding magnesium ion: D195 (= D248), E221 (= E274), E248 (= E301)
Sites not aligning to the query:
3ck5A Crystal structure of a racemase from streptomyces coelicolor a3(2) with bound magnesium
28% identity, 87% coverage: 37:412/432 of query aligns to 32:345/357 of 3ck5A
- active site: T50 (= T55), G137 (≠ D155), K164 (= K218), K166 (= K220), D195 (= D248), N197 (= N250), I220 (= I273), E221 (= E274), I243 (≠ V297), G246 (= G300), E247 (= E301), E268 (≠ Q322), D270 (= D324), H297 (= H351), G298 (= G356), V299 (≠ L357), Y315 (= Y383), E317 (≠ D385)
- binding magnesium ion: D195 (= D248), E221 (= E274), E247 (= E301)
Sites not aligning to the query:
5olcC Crystal structure of the 3,6-anhydro-d-galactonate cycloisomerase from zobellia galactanivorans (see paper)
29% identity, 49% coverage: 211:422/432 of query aligns to 141:348/351 of 5olcC
- active site: K148 (= K218), K150 (= K220), D178 (= D248), N180 (= N250), E204 (= E274), G229 (= G300), E230 (= E301), D253 (= D324), H280 (= H351), E304 (≠ S373), E309 (≠ N378)
- binding magnesium ion: D178 (= D248), E204 (= E274), E230 (= E301)
3stpA Crystal structure of a putative galactonate dehydratase
27% identity, 69% coverage: 55:353/432 of query aligns to 58:318/390 of 3stpA
- active site: L66 (≠ C63), S69 (≠ A66), S151 (≠ T190), K177 (= K218), R179 (≠ K220), P189 (≠ G223), E214 (≠ D248), Y216 (≠ N250), E240 (= E274), G265 (= G300), E266 (= E301), H267 (= H302), Q287 (= Q322), D289 (= D324), I311 (≠ V346), H316 (= H351)
- binding magnesium ion: E214 (≠ D248), E240 (= E274), E266 (= E301)
Sites not aligning to the query:
Q9RKF7 3,6-anhydro-alpha-L-galactonate cycloisomerase; AHGA cycloisomerase; EC 5.5.1.25 from Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
27% identity, 87% coverage: 37:412/432 of query aligns to 32:348/361 of Q9RKF7
- D195 (= D248) binding
- E221 (= E274) binding
- E247 (= E301) binding
Query Sequence
>BPHYT_RS20755 FitnessBrowser__BFirm:BPHYT_RS20755
MPTITRLSVRDIRFPTSRSLDGSDAMNAAPDYSAAYVTLETDSPDALTGHGLTFTIGRGN
EICVAAVEALAPLIVGKRLEDIAANMGAFWRALTSDSQLRWIGPDKGAIHLATAAVVNAA
WDLWAKAEGKPVWKLLVDMSPEELVRCLDFRYVTDAITPQEAIAMLHRHAKTRGEREKEM
LAQGYPAYTTSAGWLGYDDDKIRRLAREGVAQGWTHFKQKVGGNLDEDMRRARILREEIG
EDRKLMMDANQVWDVDEAVANMRRLAQFDPWWIEEPTSPDDILGHAAIRQRLRQIGVATG
EHCHNRVMFKQLLQAQAIDFCQVDSCRLGGLNEVIVVLLMAAKFGVPVCPHAGGVGLCEY
VQHISLFDYICVSASLENRVLEYVDHLHEHFVDPVVIRNGRYMPPQRSGYSIEMHAASLD
EYDFPEGVAWRG
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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