SitesBLAST
Comparing CA265_RS04225 FitnessBrowser__Pedo557:CA265_RS04225 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)
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)
41% identity, 100% coverage: 2:406/406 of query aligns to 6:419/443 of Q7L5Y1
- M145 (≠ E138) to T: in dbSNP:rs2612086
- S148 (≠ N141) modified: Phosphoserine
- D250 (= D243) binding
- E276 (= E269) binding
- E305 (= E296) binding
Sites not aligning to the query:
- 1:27 mutation Missing: Impairs protein solubility. Abolishes catalytic activity.
4a35A Crystal structure of human mitochondrial enolase superfamily member 1 (enosf1) (see paper)
41% identity, 100% coverage: 2:406/406 of query aligns to 7:420/441 of 4a35A
- active site: K221 (= K212), K223 (= K214), D251 (= D243), N253 (= N245), E277 (= E269), E306 (= E296), D329 (= D319), H356 (= H346), S380 (vs. gap), E387 (= E373)
- binding magnesium ion: Y188 (= Y179), D251 (= D243), E277 (= E269), E306 (= E296), Y374 (≠ H362)
4ip5A Crystal structure of l-fuconate dehydratase from silicibacter sp. Tm1040 liganded with mg and d-erythronohydroxamate
41% identity, 100% coverage: 2:406/406 of query aligns to 3:412/421 of 4ip5A
- active site: K217 (= K214), D245 (= D243), N247 (= N245), E271 (= E269), E298 (= E296), D321 (= D319), H348 (= H346), E379 (= E373)
- binding (2r,3r)-n,2,3,4-tetrahydroxybutanamide: G21 (= G19), D23 (= D21), Y31 (= Y29), K215 (= K212), K217 (= K214), D245 (= D243), N247 (= N245), E298 (= E296), H348 (= H346)
- binding magnesium ion: D245 (= D243), E271 (= E269), E298 (= E296)
4ip4A Crystal structure of l-fuconate dehydratase from silicibacter sp. Tm1040 liganded with mg
41% identity, 100% coverage: 2:406/406 of query aligns to 3:412/421 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)
41% identity, 100% coverage: 2:405/406 of query aligns to 4:414/441 of Q8P3K2
- GSD 22:24 (= GSD 19:21) binding
- Y32 (= Y29) binding
- K218 (= K212) binding
- K220 (= K214) mutation to A: Inactive.
- D248 (= D243) binding
- N250 (= N245) binding
- E274 (= E269) binding ; binding
- E301 (= E296) binding ; binding
- HAG 351:353 (≠ HVG 346:348) binding
- E382 (= E373) binding
1yeyC Crystal structure of l-fuconate dehydratase from xanthomonas campestris pv. Campestris str. Atcc 33913
41% identity, 100% coverage: 2:405/406 of query aligns to 4:414/435 of 1yeyC
- active site: T55 (= T50), T190 (= T184), K218 (= K212), K220 (= K214), D248 (= D243), N250 (= N245), E274 (= E269), G300 (= G295), E301 (= E296), D324 (= D319), P350 (= P345), H351 (= H346), A352 (≠ V347), D368 (≠ N361), K375 (vs. gap), E382 (= E373)
- binding magnesium ion: D248 (= D243), E274 (= E269), E301 (= E296)
2hxtA Crystal structure of l-fuconate dehydratase from xanthomonas campestris liganded with mg++ and d-erythronohydroxamate (see paper)
41% identity, 100% coverage: 2:405/406 of query aligns to 3:413/434 of 2hxtA
- active site: T54 (= T50), T189 (= T184), K217 (= K212), K219 (= K214), D247 (= D243), N249 (= N245), E273 (= E269), G299 (= G295), E300 (= E296), D323 (= D319), P349 (= P345), H350 (= H346), A351 (≠ V347), D367 (≠ N361), K374 (vs. gap), E381 (= E373)
- binding (2r,3r)-n,2,3,4-tetrahydroxybutanamide: G21 (= G19), D23 (= D21), Y31 (= Y29), K217 (= K212), K219 (= K214), E300 (= E296), H350 (= H346), G352 (= G348), E381 (= E373)
- binding magnesium ion: D247 (= D243), E273 (= E269), E300 (= E296)
2hxuA Crystal structure of k220a mutant of l-fuconate dehydratase from xanthomonas campestris liganded with mg++ and l-fuconate (see paper)
41% identity, 100% coverage: 2:405/406 of query aligns to 3:413/434 of 2hxuA
- active site: T54 (= T50), T189 (= T184), K217 (= K212), A219 (≠ K214), D247 (= D243), N249 (= N245), E273 (= E269), G299 (= G295), E300 (= E296), D323 (= D319), P349 (= P345), H350 (= H346), A351 (≠ V347), D367 (≠ N361), K374 (vs. gap), E381 (= E373)
- binding 6-deoxy-L-galactonic acid: G21 (= G19), D23 (= D21), Y31 (= Y29), W193 (= W188), K217 (= K212), D247 (= D243), E300 (= E296), H350 (= H346), G352 (= G348), E381 (= E373)
- binding magnesium ion: D247 (= D243), E273 (= E269), E300 (= E296)
4h19A Crystal structure of an enolase (mandelate racemase subgroup, target efi-502087) from agrobacterium tumefaciens, with bound mg and d- ribonohydroxamate, ordered loop
30% identity, 99% coverage: 2:402/406 of query aligns to 3:356/372 of 4h19A
- active site: I20 (≠ G19), T51 (= T50), T143 (= T184), K172 (= K212), K174 (= K214), D203 (= D243), N205 (= N245), E229 (= E269), G254 (= G295), E255 (= E296), Q276 (= Q317), D278 (= D319), H305 (= H346), A306 (≠ V347), G307 (= G348), E327 (= E373)
- binding (2R,3R,4R)-N,2,3,4,5-pentakis(oxidanyl)pentanamide: D22 (= D21), H25 (= H24), H52 (vs. gap), K172 (= K212), K174 (= K214), D203 (= D243), N205 (= N245), E229 (= E269), E255 (= E296), H305 (= H346), E327 (= E373)
- binding calcium ion: D268 (≠ Q309), H298 (≠ F339)
- binding magnesium ion: D203 (= D243), E229 (= E269), E255 (= E296)
2pp1A Crystal structure of l-talarate/galactarate dehydratase from salmonella typhimurium lt2 liganded with mg and l-lyxarohydroxamate (see paper)
25% identity, 88% coverage: 33:391/406 of query aligns to 61:363/395 of 2pp1A
- active site: S78 (≠ T50), K192 (= K212), K194 (= K214), D223 (= D243), N225 (= N245), E249 (= E269), G274 (= G295), E275 (= E296), D298 (= D319), H325 (= H346), E345 (= E373)
- binding (2r,3s,4r)-2,3,4-trihydroxy-5-(hydroxyamino)-5-oxopentanoic acid: K79 (≠ L51), F168 (≠ W188), K194 (= K214), E275 (= E296), H325 (= H346), E345 (= E373)
- binding magnesium ion: D223 (= D243), E249 (= E269), E275 (= E296)
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)
25% identity, 88% coverage: 33:391/406 of query aligns to 64:366/398 of Q8ZL58
- KR 82:83 (≠ LG 51:52) binding
- K195 (= K212) binding
- K197 (= K214) active site, Proton acceptor; mutation to A: Loss of dehydration activity on both L-talarate and galactarate and loss of epimerization activity.
- D226 (= D243) binding
- N228 (= N245) binding
- E252 (= E269) binding
- E278 (= E296) binding
- H328 (= H346) 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 (= E373) binding
Sites not aligning to the query:
2pp3A Crystal structure of l-talarate/galactarate dehydratase mutant k197a liganded with mg and l-glucarate (see paper)
25% identity, 88% coverage: 33:391/406 of query aligns to 61:363/395 of 2pp3A
- active site: S78 (≠ T50), K192 (= K212), A194 (≠ K214), D223 (= D243), N225 (= N245), E249 (= E269), G274 (= G295), E275 (= E296), D298 (= D319), H325 (= H346), E345 (= E373)
- binding l-glucaric acid: K79 (≠ L51), K192 (= K212), D223 (= D243), N225 (= N245), E275 (= E296), H325 (= H346), E345 (= E373), F347 (≠ I375)
- binding magnesium ion: D223 (= D243), E249 (= E269), E275 (= E296)
Sites not aligning to the query:
2og9A Crystal structure of mandelate racemase/muconate lactonizing enzyme from polaromonas sp. Js666
30% identity, 55% coverage: 182:406/406 of query aligns to 130:346/363 of 2og9A
- active site: T132 (= T184), K160 (= K212), K162 (= K214), D191 (= D243), N193 (= N245), E217 (= E269), G242 (= G295), E243 (= E296), M264 (≠ Q317), D266 (= D319), H293 (= H346), F294 (≠ V347), A295 (≠ G348), E313 (= E373)
- binding calcium ion: A232 (= A284), F235 (≠ I287)
Sites not aligning to the query:
3cb3A Crystal structure of l-talarate dehydratase from polaromonas sp. Js666 complexed with mg and l-glucarate
31% identity, 54% coverage: 182:400/406 of query aligns to 141:351/373 of 3cb3A
- active site: T143 (= T184), K171 (= K212), K173 (= K214), D202 (= D243), N204 (= N245), E228 (= E269), G253 (= G295), E254 (= E296), M275 (≠ Q317), D277 (= D319), H304 (= H346), F305 (≠ V347), A306 (≠ G348), E324 (= E373)
- binding l-glucaric acid: K171 (= K212), K173 (= K214), D202 (= D243), E254 (= E296), H304 (= H346)
- binding magnesium ion: D202 (= D243), E228 (= E269), A243 (= A284), F246 (≠ I287), E254 (= E296)
Sites not aligning to the query:
5xd8B Crystal structure analysis of 3,6-anhydro-l-galactonate cycloisomerase (see paper)
27% identity, 63% coverage: 102:358/406 of query aligns to 99:310/367 of 5xd8B
- active site: G140 (= G173), K167 (= K212), K169 (= K214), D198 (= D243), N200 (= N245), E224 (= E269), G249 (= G295), E250 (= E296), Q271 (= Q317), D273 (= D319), H300 (= H346), G301 (≠ D349), M302 (= M350)
- binding magnesium ion: D198 (= D243), E224 (= E269), E250 (= E296)
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)
23% identity, 100% coverage: 1:405/406 of query aligns to 1:350/361 of Q9RKF7
- D195 (= D243) binding
- E221 (= E269) binding
- E247 (= E296) binding
3ck5A Crystal structure of a racemase from streptomyces coelicolor a3(2) with bound magnesium
23% identity, 99% coverage: 1:400/406 of query aligns to 1:342/357 of 3ck5A
- active site: T19 (≠ S20), T50 (= T50), G137 (≠ N141), K164 (= K212), K166 (= K214), D195 (= D243), N197 (= N245), I220 (≠ V268), E221 (= E269), I243 (≠ L292), G246 (= G295), E247 (= E296), E268 (≠ Q317), D270 (= D319), H297 (= H346), G298 (≠ H354), V299 (≠ Q355), Y315 (≠ F371), E317 (= E373)
- binding magnesium ion: D195 (= D243), E221 (= E269), E247 (= E296)
3op2A Crystal structure of putative mandelate racemase from bordetella bronchiseptica rb50 complexed with 2-oxoglutarate/phosphate
30% identity, 55% coverage: 178:400/406 of query aligns to 132:354/375 of 3op2A
- active site: S138 (≠ T184), K165 (= K212), K167 (= K214), D195 (= D243), N197 (= N245), E221 (= E269), G247 (= G295), E248 (= E296), N249 (≠ H297), Q269 (= Q317), D271 (= D319), H298 (= H346), T299 (≠ V347), F300 (vs. gap), E323 (≠ L372), I326 (= I375), H328 (= H377)
- binding 2-oxoglutaric acid: K165 (= K212), K167 (= K214), D195 (= D243), E248 (= E296), H298 (= H346), E323 (≠ L372)
- binding magnesium ion: D195 (= D243), E221 (= E269), E248 (= E296)
Sites not aligning to the query:
3ozmD Crystal structure of enolase superfamily member from bordetella bronchiseptica complexed with mg, m-xylarate and l-lyxarate
30% identity, 55% coverage: 178:400/406 of query aligns to 137:359/381 of 3ozmD
- active site: S143 (≠ T184), K170 (= K212), K172 (= K214), D200 (= D243), N202 (= N245), E226 (= E269), G252 (= G295), E253 (= E296), N254 (≠ H297), Q274 (= Q317), D276 (= D319), H303 (= H346), T304 (≠ V347), F305 (vs. gap), E328 (≠ L372), I331 (= I375), H333 (= H377)
- binding L-arabinaric acid: K172 (= K214), D200 (= D243), N202 (= N245), E253 (= E296), H303 (= H346), F305 (vs. gap), E328 (≠ L372)
- binding magnesium ion: D200 (= D243), E226 (= E269), E253 (= E296)
Sites not aligning to the query:
3ozmA Crystal structure of enolase superfamily member from bordetella bronchiseptica complexed with mg, m-xylarate and l-lyxarate
30% identity, 55% coverage: 178:400/406 of query aligns to 137:359/386 of 3ozmA
- active site: S143 (≠ T184), K170 (= K212), K172 (= K214), D200 (= D243), N202 (= N245), E226 (= E269), G252 (= G295), E253 (= E296), N254 (≠ H297), Q274 (= Q317), D276 (= D319), H303 (= H346), T304 (≠ V347), F305 (vs. gap), E328 (≠ L372), I331 (= I375), H333 (= H377)
- binding D-xylaric acid: Y146 (≠ G187), K170 (= K212), K172 (= K214), D200 (= D243), N202 (= N245), E253 (= E296), H303 (= H346), F305 (vs. gap), E328 (≠ L372)
- binding magnesium ion: D200 (= D243), E226 (= E269), E253 (= E296)
Sites not aligning to the query:
Query Sequence
>CA265_RS04225 FitnessBrowser__Pedo557:CA265_RS04225
MINKIEISDKRFELSTGAGSDAIHKDPQYSYAVTNLTNENGITGTGLAFTLGAGNDLVCN
AAQFYANKLKGQDIEELMSDFGQTFRTLSNEQQFRWLGPHKGVVHLGLASVTNACYDLWA
KKRGVPLWKLLIDLSPEEIVNTLDLSYLEDVLTKEEAIAMLQSQTDSKKSREGILDTGYP
GYDTSVGWFNYDDEKVRENCKKAIANGFTAMKLKVGSADPKRDIRRANIVREVAGESSKV
MLDANQQWTLPQAISICNELKNMNPFWVEEPTHPDDVLAHQTLAREIAPVKLALGEHVPN
RIIFKNYLQTGCTGFAQVDAVRVGGVSEFITISLLCKKFGVPVVPHVGDMGQLHQHLVLF
NHIAMGHEALFLEHIPHLKQHFKHPIKIEKGVYITPQEAGSSCDLK
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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