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Comparing RR42_RS34985 FitnessBrowser__Cup4G11:RR42_RS34985 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)
2pp1A Crystal structure of l-talarate/galactarate dehydratase from salmonella typhimurium lt2 liganded with mg and l-lyxarohydroxamate (see paper)
38% identity, 93% coverage: 8:350/368 of query aligns to 28:375/395 of 2pp1A
- active site: K45 (≠ Q26), S78 (≠ T52), K192 (= K167), K194 (= K169), D223 (= D198), N225 (= N200), E249 (= E224), G274 (= G249), E275 (= E250), D298 (= D273), H325 (= H300), E345 (= E320)
- binding (2r,3s,4r)-2,3,4-trihydroxy-5-(hydroxyamino)-5-oxopentanoic acid: D43 (= D23), K45 (≠ Q26), K79 (≠ I53), F168 (≠ W143), K194 (= K169), E275 (= E250), H325 (= H300), E345 (= E320)
- binding magnesium ion: D223 (= D198), E249 (= E224), E275 (= E250)
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)
38% identity, 93% coverage: 8:350/368 of query aligns to 31:378/398 of Q8ZL58
- DA-K 46:48 (≠ DAIQ 23:26) binding
- KR 82:83 (≠ IG 53:54) binding
- K195 (= K167) binding
- K197 (= K169) active site, Proton acceptor; mutation to A: Loss of dehydration activity on both L-talarate and galactarate and loss of epimerization activity.
- D226 (= D198) binding
- N228 (= N200) binding
- E252 (= E224) binding
- E278 (= E250) binding
- H328 (= H300) 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 (= E320) binding
2pp3A Crystal structure of l-talarate/galactarate dehydratase mutant k197a liganded with mg and l-glucarate (see paper)
38% identity, 93% coverage: 8:350/368 of query aligns to 28:375/395 of 2pp3A
- active site: K45 (≠ Q26), S78 (≠ T52), K192 (= K167), A194 (≠ K169), D223 (= D198), N225 (= N200), E249 (= E224), G274 (= G249), E275 (= E250), D298 (= D273), H325 (= H300), E345 (= E320)
- binding l-glucaric acid: D43 (= D23), K79 (≠ I53), K192 (= K167), D223 (= D198), N225 (= N200), E275 (= E250), H325 (= H300), E345 (= E320), F347 (≠ I322)
- binding magnesium ion: D223 (= D198), E249 (= E224), E275 (= E250)
5xd8B Crystal structure analysis of 3,6-anhydro-l-galactonate cycloisomerase (see paper)
36% identity, 98% coverage: 1:362/368 of query aligns to 1:362/367 of 5xd8B
- active site: S22 (= S22), T53 (= T52), G140 (= G141), K167 (= K167), K169 (= K169), D198 (= D198), N200 (= N200), E224 (= E224), G249 (= G249), E250 (= E250), Q271 (= Q271), D273 (= D273), H300 (= H300), G301 (≠ F301), M302 (≠ L302), W317 (= W318), E319 (= E320), P324 (≠ Q324)
- binding magnesium ion: D198 (= D198), E224 (= E224), E250 (= E250)
3cb3A Crystal structure of l-talarate dehydratase from polaromonas sp. Js666 complexed with mg and l-glucarate
38% identity, 95% coverage: 2:350/368 of query aligns to 1:354/373 of 3cb3A
- active site: K24 (≠ Q26), S57 (≠ T52), T143 (= T139), K171 (= K167), K173 (= K169), D202 (= D198), N204 (= N200), E228 (= E224), G253 (= G249), E254 (= E250), M275 (≠ Q271), D277 (= D273), H304 (= H300), F305 (= F301), A306 (≠ L302), E324 (= E320)
- binding l-glucaric acid: K171 (= K167), K173 (= K169), D202 (= D198), E254 (= E250), H304 (= H300)
- binding magnesium ion: D202 (= D198), E228 (= E224), A243 (= A239), F246 (≠ T242), E254 (= E250)
2og9A Crystal structure of mandelate racemase/muconate lactonizing enzyme from polaromonas sp. Js666
39% identity, 86% coverage: 35:350/368 of query aligns to 29:343/363 of 2og9A
- active site: S46 (≠ T52), T132 (= T139), K160 (= K167), K162 (= K169), D191 (= D198), N193 (= N200), E217 (= E224), G242 (= G249), E243 (= E250), M264 (≠ Q271), D266 (= D273), H293 (= H300), F294 (= F301), A295 (≠ L302), E313 (= E320)
- binding calcium ion: A232 (= A239), F235 (≠ T242)
3ck5A Crystal structure of a racemase from streptomyces coelicolor a3(2) with bound magnesium
38% identity, 97% coverage: 6:362/368 of query aligns to 5:357/357 of 3ck5A
- active site: T19 (≠ S22), T50 (= T52), G137 (≠ T139), K164 (= K167), K166 (= K169), D195 (= D198), N197 (= N200), I220 (≠ F223), E221 (= E224), I243 (= I246), G246 (= G249), E247 (= E250), E268 (≠ Q271), D270 (= D273), H297 (= H300), G298 (≠ F301), V299 (≠ L302), Y315 (≠ W318), E317 (= E320)
- binding magnesium ion: D195 (= D198), E221 (= E224), E247 (= E250)
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)
38% identity, 97% coverage: 6:363/368 of query aligns to 5:361/361 of Q9RKF7
- D195 (= D198) binding
- E221 (= E224) binding
- E247 (= E250) binding
4h19A Crystal structure of an enolase (mandelate racemase subgroup, target efi-502087) from agrobacterium tumefaciens, with bound mg and d- ribonohydroxamate, ordered loop
36% identity, 94% coverage: 1:347/368 of query aligns to 1:354/372 of 4h19A
- active site: I20 (≠ R21), T51 (= T52), T143 (= T139), K172 (= K167), K174 (= K169), D203 (= D198), N205 (= N200), E229 (= E224), G254 (= G249), E255 (= E250), Q276 (= Q271), D278 (= D273), H305 (= H300), A306 (≠ F301), G307 (vs. gap), E327 (= E320)
- binding (2R,3R,4R)-N,2,3,4,5-pentakis(oxidanyl)pentanamide: D22 (= D23), H25 (≠ Q26), H52 (≠ I53), K172 (= K167), K174 (= K169), D203 (= D198), N205 (= N200), E229 (= E224), E255 (= E250), H305 (= H300), E327 (= E320)
- binding calcium ion: D268 (≠ R263), H298 (= H293)
- binding magnesium ion: D203 (= D198), E229 (= E224), E255 (= E250)
3op2A Crystal structure of putative mandelate racemase from bordetella bronchiseptica rb50 complexed with 2-oxoglutarate/phosphate
35% identity, 96% coverage: 1:354/368 of query aligns to 2:361/375 of 3op2A
- active site: M20 (≠ V19), G53 (= G57), D56 (≠ V60), S138 (≠ T139), K165 (= K167), K167 (= K169), D195 (= D198), N197 (= N200), E221 (= E224), G247 (= G249), E248 (= E250), N249 (≠ S251), Q269 (= Q271), D271 (= D273), H298 (= H300), T299 (≠ F301), F300 (≠ L302), E323 (= E320), I326 (= I322), H328 (≠ Q324)
- binding 2-oxoglutaric acid: K165 (= K167), K167 (= K169), D195 (= D198), E248 (= E250), H298 (= H300), E323 (= E320)
- binding magnesium ion: D195 (= D198), E221 (= E224), E248 (= E250)
3ozmA Crystal structure of enolase superfamily member from bordetella bronchiseptica complexed with mg, m-xylarate and l-lyxarate
34% identity, 96% coverage: 1:354/368 of query aligns to 2:366/386 of 3ozmA
- active site: M20 (≠ V19), G53 (= G57), D56 (≠ V60), S143 (≠ T139), K170 (= K167), K172 (= K169), D200 (= D198), N202 (= N200), E226 (= E224), G252 (= G249), E253 (= E250), N254 (≠ S251), Q274 (= Q271), D276 (= D273), H303 (= H300), T304 (≠ F301), F305 (≠ L302), E328 (= E320), I331 (= I322), H333 (≠ Q324)
- binding D-xylaric acid: S24 (≠ D23), K29 (≠ F28), Y146 (≠ G142), K170 (= K167), K172 (= K169), D200 (= D198), N202 (= N200), E253 (= E250), H303 (= H300), F305 (≠ L302), E328 (= E320)
- binding magnesium ion: D200 (= D198), E226 (= E224), E253 (= E250)
3ozmD Crystal structure of enolase superfamily member from bordetella bronchiseptica complexed with mg, m-xylarate and l-lyxarate
34% identity, 96% coverage: 1:354/368 of query aligns to 2:366/381 of 3ozmD
- active site: M20 (≠ V19), G53 (= G57), D56 (≠ V60), S143 (≠ T139), K170 (= K167), K172 (= K169), D200 (= D198), N202 (= N200), E226 (= E224), G252 (= G249), E253 (= E250), N254 (≠ S251), Q274 (= Q271), D276 (= D273), H303 (= H300), T304 (≠ F301), F305 (≠ L302), E328 (= E320), I331 (= I322), H333 (≠ Q324)
- binding L-arabinaric acid: K172 (= K169), D200 (= D198), N202 (= N200), E253 (= E250), H303 (= H300), F305 (≠ L302), E328 (= E320)
- binding magnesium ion: D200 (= D198), E226 (= E224), E253 (= E250)
6vimA P. Putida mandelate racemase co-crystallized with phenylboronic acid (see paper)
30% identity, 95% coverage: 13:362/368 of query aligns to 12:357/357 of 6vimA
- active site: V20 (≠ R21), S137 (≠ T139), K162 (= K167), K164 (= K169), D193 (= D198), N195 (= N200), E219 (= E224), G244 (= G249), E245 (= E250), D268 (= D273), H295 (= H300), L296 (≠ F301), F297 (≠ L302), E315 (= E320)
- binding magnesium ion: D193 (= D198), E219 (= E224), E245 (= E250)
- binding phenyl boronic acid: V20 (≠ R21), K162 (= K167), K164 (= K169), D193 (= D198), E245 (= E250), H295 (= H300), L296 (≠ F301), E315 (= E320), L317 (≠ I322)
4x2pA P. Putida mandelate racemase in complex with 3-hydroxypyruvate (see paper)
30% identity, 95% coverage: 13:362/368 of query aligns to 12:357/357 of 4x2pA
- active site: V20 (≠ R21), S137 (≠ T139), K162 (= K167), K164 (= K169), D193 (= D198), N195 (= N200), E219 (= E224), G244 (= G249), E245 (= E250), D268 (= D273), M292 (≠ I297), H295 (= H300), L296 (≠ F301), F297 (≠ L302), A311 (= A316), E315 (= E320)
- binding 3-hydroxypyruvic acid: K162 (= K167), K164 (= K169), D193 (= D198), H295 (= H300), E315 (= E320)
- binding magnesium ion: D193 (= D198), E219 (= E224), E245 (= E250)
4m6uA P. Putida mandelate racemase co-crystallized with tartronic acid (see paper)
30% identity, 95% coverage: 13:362/368 of query aligns to 12:357/357 of 4m6uA
- active site: V20 (≠ R21), S137 (≠ T139), K162 (= K167), K164 (= K169), D193 (= D198), N195 (= N200), E219 (= E224), G244 (= G249), E245 (= E250), D268 (= D273), M292 (≠ I297), H295 (= H300), L296 (≠ F301), F297 (≠ L302), A311 (= A316), E315 (= E320)
- binding magnesium ion: D193 (= D198), E219 (= E224), E245 (= E250)
- binding tartronate: K162 (= K167), K164 (= K169), D193 (= D198), E245 (= E250), H295 (= H300), E315 (= E320)
4fp1A P. Putida mandelate racemase co-crystallized with 3,3,3-trifluoro-2- hydroxy-2-(trifluoromethyl) propionic acid (see paper)
30% identity, 95% coverage: 13:362/368 of query aligns to 12:357/357 of 4fp1A
- active site: V20 (≠ R21), S137 (≠ T139), K162 (= K167), K164 (= K169), D193 (= D198), N195 (= N200), E219 (= E224), G244 (= G249), E245 (= E250), D268 (= D273), M292 (≠ I297), H295 (= H300), L296 (≠ F301), F297 (≠ L302), A311 (= A316), E315 (= E320)
- binding 3,3,3-trifluoro-2-hydroxy-2-(trifluoromethyl)propanoic acid: V20 (≠ R21), K164 (= K169), H295 (= H300), L296 (≠ F301)
- binding magnesium ion: D193 (= D198), E219 (= E224), E245 (= E250)
3uxlA P. Putida mandelate racemase co-crystallized with the intermediate analogue cupferron (see paper)
30% identity, 95% coverage: 13:362/368 of query aligns to 12:357/357 of 3uxlA
- active site: V20 (≠ R21), S137 (≠ T139), K162 (= K167), K164 (= K169), D193 (= D198), N195 (= N200), E219 (= E224), G244 (= G249), E245 (= E250), D268 (= D273), M292 (≠ I297), H295 (= H300), L296 (≠ F301), F297 (≠ L302), A311 (= A316), E315 (= E320)
- binding 1-hydroxy-2-oxo-1-phenylhydrazine: K162 (= K167), K164 (= K169), D193 (= D198), N195 (= N200), E245 (= E250), H295 (= H300)
- binding magnesium ion: D193 (= D198), E219 (= E224), E245 (= E250)
3uxkA P. Putida mandelate racemase co-crystallized with the intermediate analogue benzohydroxamate (see paper)
30% identity, 95% coverage: 13:362/368 of query aligns to 12:357/357 of 3uxkA
- active site: V20 (≠ R21), S137 (≠ T139), K162 (= K167), K164 (= K169), D193 (= D198), N195 (= N200), E219 (= E224), G244 (= G249), E245 (= E250), D268 (= D273), M292 (≠ I297), H295 (= H300), L296 (≠ F301), F297 (≠ L302), A311 (= A316), E315 (= E320)
- binding benzhydroxamic acid: V20 (≠ R21), K162 (= K167), K164 (= K169), D193 (= D198), N195 (= N200), E245 (= E250), H295 (= H300), L317 (≠ I322)
- binding magnesium ion: D193 (= D198), E219 (= E224), E245 (= E250)
2mnrA Mechanism of the reaction catalyzed by mandelate racemase. 2. Crystal structure of mandelate racemase at 2.5 angstroms resolution: identification of the active site and possible catalytic residues (see paper)
30% identity, 95% coverage: 13:362/368 of query aligns to 12:357/357 of 2mnrA
- active site: V20 (≠ R21), S137 (≠ T139), K162 (= K167), K164 (= K169), D193 (= D198), N195 (= N200), E219 (= E224), G244 (= G249), E245 (= E250), D268 (= D273), M292 (≠ I297), H295 (= H300), L296 (≠ F301), F297 (≠ L302), A311 (= A316), E315 (= E320)
- binding manganese (ii) ion: D193 (= D198), E219 (= E224), E245 (= E250)
P11444 Mandelate racemase; MR; EC 5.1.2.2 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 3 papers)
30% identity, 95% coverage: 13:362/368 of query aligns to 14:359/359 of P11444
- K166 (= K169) mutation K->A,M,Q: Loss of activity.
- D195 (= D198) binding
- E221 (= E224) binding
- E247 (= E250) binding
- H297 (= H300) mutation to N: Loss of activity.
- E317 (= E320) binding ; mutation to Q: Reduces activity 10000-fold.
Query Sequence
>RR42_RS34985 FitnessBrowser__Cup4G11:RR42_RS34985
MSATIVQVELLQVDLPPRVPRSDAIQSFVMQETPMVRIRCDDGAEGTGYAYTIGTGGSSV
MALLRDHLAPRLIGRDPAQIEAIWRELLFATHATSVGAITSLALAAIDTALWDWRCRRDG
QPLWLAAGGAQPRVPVYTTEGGWLHLDADTLVSEAVAAREAGFRGAKLKVGRARASEDVA
RLAAVRDAVGDGFELMVDANQCFTAAEAIRRAPHYAELGIAWFEEPLPADDIGGHVRLAA
STSVPIAVGESLYSPGQFAEYVRQGACGIVQADVARIGGITPWLKVAHLAEAHNLSICPH
FLMELHVSLCAAVPNAAWVEYIPQLDEIAASSVRIEAGHAIAPDAPGLGIEWDWAAIGRR
TVARALVS
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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