SitesBLAST
Comparing RR42_RS22655 FitnessBrowser__Cup4G11:RR42_RS22655 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)
3cb3A Crystal structure of l-talarate dehydratase from polaromonas sp. Js666 complexed with mg and l-glucarate
83% identity, 97% coverage: 12:384/385 of query aligns to 1:373/373 of 3cb3A
- active site: K24 (= K35), S57 (≠ A68), T143 (= T154), K171 (= K182), K173 (= K184), D202 (= D213), N204 (= N215), E228 (= E239), G253 (= G264), E254 (= E265), M275 (= M286), D277 (= D288), H304 (= H315), F305 (= F316), A306 (= A317), E324 (= E335)
- binding l-glucaric acid: K171 (= K182), K173 (= K184), D202 (= D213), E254 (= E265), H304 (= H315)
- binding magnesium ion: D202 (= D213), E228 (= E239), A243 (= A254), F246 (= F257), E254 (= E265)
2og9A Crystal structure of mandelate racemase/muconate lactonizing enzyme from polaromonas sp. Js666
80% identity, 97% coverage: 12:384/385 of query aligns to 2:362/363 of 2og9A
- active site: S46 (≠ A68), T132 (= T154), K160 (= K182), K162 (= K184), D191 (= D213), N193 (= N215), E217 (= E239), G242 (= G264), E243 (= E265), M264 (= M286), D266 (= D288), H293 (= H315), F294 (= F316), A295 (= A317), E313 (= E335)
- binding calcium ion: A232 (= A254), F235 (= F257)
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)
66% identity, 99% coverage: 2:384/385 of query aligns to 17:397/398 of Q8ZL58
- DAK 46:48 (= DAK 33:35) binding
- KR 82:83 (= KR 69:70) binding
- K195 (= K182) binding
- K197 (= K184) active site, Proton acceptor; mutation to A: Loss of dehydration activity on both L-talarate and galactarate and loss of epimerization activity.
- D226 (= D213) binding
- N228 (= N215) binding
- E252 (= E239) binding
- E278 (= E265) binding
- H328 (= H315) 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 (= E335) binding
2pp1A Crystal structure of l-talarate/galactarate dehydratase from salmonella typhimurium lt2 liganded with mg and l-lyxarohydroxamate (see paper)
66% identity, 99% coverage: 2:384/385 of query aligns to 14:394/395 of 2pp1A
- active site: K45 (= K35), S78 (≠ A68), K192 (= K182), K194 (= K184), D223 (= D213), N225 (= N215), E249 (= E239), G274 (= G264), E275 (= E265), D298 (= D288), H325 (= H315), E345 (= E335)
- binding (2r,3s,4r)-2,3,4-trihydroxy-5-(hydroxyamino)-5-oxopentanoic acid: D43 (= D33), K45 (= K35), K79 (= K69), F168 (= F158), K194 (= K184), E275 (= E265), H325 (= H315), E345 (= E335)
- binding magnesium ion: D223 (= D213), E249 (= E239), E275 (= E265)
2pp3A Crystal structure of l-talarate/galactarate dehydratase mutant k197a liganded with mg and l-glucarate (see paper)
66% identity, 99% coverage: 2:384/385 of query aligns to 14:394/395 of 2pp3A
- active site: K45 (= K35), S78 (≠ A68), K192 (= K182), A194 (≠ K184), D223 (= D213), N225 (= N215), E249 (= E239), G274 (= G264), E275 (= E265), D298 (= D288), H325 (= H315), E345 (= E335)
- binding l-glucaric acid: D43 (= D33), K79 (= K69), K192 (= K182), D223 (= D213), N225 (= N215), E275 (= E265), H325 (= H315), E345 (= E335), F347 (= F337)
- binding magnesium ion: D223 (= D213), E249 (= E239), E275 (= E265)
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, 91% coverage: 14:362/385 of query aligns to 2:354/372 of 4h19A
- active site: I20 (= I31), T51 (≠ G73), T143 (= T154), K172 (= K182), K174 (= K184), D203 (= D213), N205 (= N215), E229 (= E239), G254 (= G264), E255 (= E265), Q276 (≠ M286), D278 (= D288), H305 (= H315), A306 (≠ F316), G307 (≠ A317), E327 (= E335)
- binding (2R,3R,4R)-N,2,3,4,5-pentakis(oxidanyl)pentanamide: D22 (= D33), H25 (≠ K42), H52 (≠ P74), K172 (= K182), K174 (= K184), D203 (= D213), N205 (= N215), E229 (= E239), E255 (= E265), H305 (= H315), E327 (= E335)
- binding calcium ion: D268 (≠ R278), H298 (≠ A308)
- binding magnesium ion: D203 (= D213), E229 (= E239), E255 (= E265)
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)
35% identity, 93% coverage: 15:373/385 of query aligns to 2:356/361 of Q9RKF7
- D195 (= D213) binding
- E221 (= E239) binding
- E247 (= E265) binding
3ck5A Crystal structure of a racemase from streptomyces coelicolor a3(2) with bound magnesium
35% identity, 93% coverage: 15:373/385 of query aligns to 2:353/357 of 3ck5A
- active site: T19 (≠ S32), T50 (≠ A68), G137 (= G156), K164 (= K182), K166 (= K184), D195 (= D213), N197 (= N215), I220 (= I238), E221 (= E239), I243 (= I261), G246 (= G264), E247 (= E265), E268 (≠ M286), D270 (= D288), H297 (= H315), G298 (≠ F316), V299 (≠ A317), Y315 (≠ W333), E317 (= E335)
- binding magnesium ion: D195 (= D213), E221 (= E239), E247 (= E265)
5xd8B Crystal structure analysis of 3,6-anhydro-l-galactonate cycloisomerase (see paper)
34% identity, 75% coverage: 82:368/385 of query aligns to 68:353/367 of 5xd8B
- active site: G140 (= G156), K167 (= K182), K169 (= K184), D198 (= D213), N200 (= N215), E224 (= E239), G249 (= G264), E250 (= E265), Q271 (≠ M286), D273 (= D288), H300 (= H315), G301 (≠ F316), M302 (≠ A317), W317 (= W333), E319 (= E335), P324 (≠ L340)
- binding magnesium ion: D198 (= D213), E224 (= E239), E250 (= E265)
Sites not aligning to the query:
3ugvF Crystal structure of an enolase from alpha pretobacterium bal199 (efi target efi-501650) with bound mg
31% identity, 87% coverage: 37:371/385 of query aligns to 20:357/364 of 3ugvF
- active site: V20 (≠ L37), P51 (≠ S66), P54 (≠ K69), A95 (≠ S112), S137 (≠ T154), K168 (= K182), R170 (≠ K184), D199 (= D213), N201 (= N215), E225 (= E239), G250 (= G264), E251 (= E265), N252 (≠ M266), M272 (= M286), D274 (= D288), A293 (≠ H307), H301 (= H315), L302 (≠ F316), Y303 (≠ A317), E321 (= E335)
- binding magnesium ion: D199 (= D213), E225 (= E239), R240 (≠ A254), L243 (≠ F257), E251 (= E265)
P11444 Mandelate racemase; MR; EC 5.1.2.2 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 3 papers)
28% identity, 91% coverage: 15:365/385 of query aligns to 6:347/359 of P11444
- K166 (= K184) mutation K->A,M,Q: Loss of activity.
- D195 (= D213) binding
- E221 (= E239) binding
- E247 (= E265) binding
- H297 (= H315) mutation to N: Loss of activity.
- E317 (= E335) binding ; mutation to Q: Reduces activity 10000-fold.
7mqxE P. Putida mandelate racemase forms an oxobenzoxaborole adduct with 2- formylphenylboronic acid (see paper)
28% identity, 91% coverage: 15:365/385 of query aligns to 5:346/358 of 7mqxE
- binding magnesium ion: D194 (= D213), E220 (= E239), E246 (= E265)
- binding (3S)-2,1-benzoxaborole-1,3(3H)-diol: V21 (≠ I31), K165 (= K184), D194 (= D213), N196 (= N215), E246 (= E265), H296 (= H315), E316 (= E335)
6vimA P. Putida mandelate racemase co-crystallized with phenylboronic acid (see paper)
28% identity, 91% coverage: 15:365/385 of query aligns to 4:345/357 of 6vimA
- active site: V20 (≠ I31), S137 (≠ T154), K162 (= K182), K164 (= K184), D193 (= D213), N195 (= N215), E219 (= E239), G244 (= G264), E245 (= E265), D268 (= D288), H295 (= H315), L296 (≠ F316), F297 (≠ A317), E315 (= E335)
- binding magnesium ion: D193 (= D213), E219 (= E239), E245 (= E265)
- binding phenyl boronic acid: V20 (≠ I31), K162 (= K182), K164 (= K184), D193 (= D213), E245 (= E265), H295 (= H315), L296 (≠ F316), E315 (= E335), L317 (≠ F337)
4x2pA P. Putida mandelate racemase in complex with 3-hydroxypyruvate (see paper)
28% identity, 91% coverage: 15:365/385 of query aligns to 4:345/357 of 4x2pA
- active site: V20 (≠ I31), S137 (≠ T154), K162 (= K182), K164 (= K184), D193 (= D213), N195 (= N215), E219 (= E239), G244 (= G264), E245 (= E265), D268 (= D288), M292 (≠ I312), H295 (= H315), L296 (≠ F316), F297 (≠ A317), A311 (≠ E331), E315 (= E335)
- binding 3-hydroxypyruvic acid: K162 (= K182), K164 (= K184), D193 (= D213), H295 (= H315), E315 (= E335)
- binding magnesium ion: D193 (= D213), E219 (= E239), E245 (= E265)
4m6uA P. Putida mandelate racemase co-crystallized with tartronic acid (see paper)
28% identity, 91% coverage: 15:365/385 of query aligns to 4:345/357 of 4m6uA
- active site: V20 (≠ I31), S137 (≠ T154), K162 (= K182), K164 (= K184), D193 (= D213), N195 (= N215), E219 (= E239), G244 (= G264), E245 (= E265), D268 (= D288), M292 (≠ I312), H295 (= H315), L296 (≠ F316), F297 (≠ A317), A311 (≠ E331), E315 (= E335)
- binding magnesium ion: D193 (= D213), E219 (= E239), E245 (= E265)
- binding tartronate: K162 (= K182), K164 (= K184), D193 (= D213), E245 (= E265), H295 (= H315), E315 (= E335)
4fp1A P. Putida mandelate racemase co-crystallized with 3,3,3-trifluoro-2- hydroxy-2-(trifluoromethyl) propionic acid (see paper)
28% identity, 91% coverage: 15:365/385 of query aligns to 4:345/357 of 4fp1A
- active site: V20 (≠ I31), S137 (≠ T154), K162 (= K182), K164 (= K184), D193 (= D213), N195 (= N215), E219 (= E239), G244 (= G264), E245 (= E265), D268 (= D288), M292 (≠ I312), H295 (= H315), L296 (≠ F316), F297 (≠ A317), A311 (≠ E331), E315 (= E335)
- binding 3,3,3-trifluoro-2-hydroxy-2-(trifluoromethyl)propanoic acid: V20 (≠ I31), K164 (= K184), H295 (= H315), L296 (≠ F316)
- binding magnesium ion: D193 (= D213), E219 (= E239), E245 (= E265)
3uxlA P. Putida mandelate racemase co-crystallized with the intermediate analogue cupferron (see paper)
28% identity, 91% coverage: 15:365/385 of query aligns to 4:345/357 of 3uxlA
- active site: V20 (≠ I31), S137 (≠ T154), K162 (= K182), K164 (= K184), D193 (= D213), N195 (= N215), E219 (= E239), G244 (= G264), E245 (= E265), D268 (= D288), M292 (≠ I312), H295 (= H315), L296 (≠ F316), F297 (≠ A317), A311 (≠ E331), E315 (= E335)
- binding 1-hydroxy-2-oxo-1-phenylhydrazine: K162 (= K182), K164 (= K184), D193 (= D213), N195 (= N215), E245 (= E265), H295 (= H315)
- binding magnesium ion: D193 (= D213), E219 (= E239), E245 (= E265)
3uxkA P. Putida mandelate racemase co-crystallized with the intermediate analogue benzohydroxamate (see paper)
28% identity, 91% coverage: 15:365/385 of query aligns to 4:345/357 of 3uxkA
- active site: V20 (≠ I31), S137 (≠ T154), K162 (= K182), K164 (= K184), D193 (= D213), N195 (= N215), E219 (= E239), G244 (= G264), E245 (= E265), D268 (= D288), M292 (≠ I312), H295 (= H315), L296 (≠ F316), F297 (≠ A317), A311 (≠ E331), E315 (= E335)
- binding benzhydroxamic acid: V20 (≠ I31), K162 (= K182), K164 (= K184), D193 (= D213), N195 (= N215), E245 (= E265), H295 (= H315), L317 (≠ F337)
- binding magnesium ion: D193 (= D213), E219 (= E239), E245 (= E265)
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)
28% identity, 91% coverage: 15:365/385 of query aligns to 4:345/357 of 2mnrA
- active site: V20 (≠ I31), S137 (≠ T154), K162 (= K182), K164 (= K184), D193 (= D213), N195 (= N215), E219 (= E239), G244 (= G264), E245 (= E265), D268 (= D288), M292 (≠ I312), H295 (= H315), L296 (≠ F316), F297 (≠ A317), A311 (≠ E331), E315 (= E335)
- binding manganese (ii) ion: D193 (= D213), E219 (= E239), E245 (= E265)
1mdlA Mandelate racemase mutant k166r co-crystallized with (r)-mandelate (see paper)
28% identity, 91% coverage: 15:365/385 of query aligns to 4:345/357 of 1mdlA
- active site: V20 (≠ I31), S137 (≠ T154), K162 (= K182), R164 (≠ K184), D193 (= D213), N195 (= N215), E219 (= E239), G244 (= G264), E245 (= E265), D268 (= D288), M292 (≠ I312), H295 (= H315), L296 (≠ F316), F297 (≠ A317), A311 (≠ E331), E315 (= E335)
- binding magnesium ion: D193 (= D213), E219 (= E239), E245 (= E265)
- binding (r)-mandelic acid: V20 (≠ I31), F50 (≠ Y67), R164 (≠ K184)
- binding (s)-mandelic acid: K162 (= K182), R164 (≠ K184), D193 (= D213), E245 (= E265), H295 (= H315), E315 (= E335)
Query Sequence
>RR42_RS22655 FitnessBrowser__Cup4G11:RR42_RS22655
MTTQHQPKTGANDNIASIRLSSVYLPLATPISDAKVLTGRQKPMTEIAILFAEIETEGGD
KGLGFSYAKRAGGPGQFAHAREIAPALIGEDANDIARLWNKLIWAGASVGRSGLATQAIG
AFDVALWDLKARRANLPLAKLLGAHRDSVKCYNTSGGFLHTPLDQLLMNASKSVEKGIGG
IKLKVGQPDCAADIQRVETVRKHLGDGFALMVDANQQWDRPTAQRMCRILEQFNLIWIEE
PLDAYDSEGHAALAAQFDTPIATGEMLTSVAEHWDLIRHRAADYLMPDGPRVGGITPFLT
VATLADHAGLMIAPHFAMELHVHLAAAYPREPWVEHFEWLEPLFNERLEIKDGRMLVPTR
PGIGVSLSGQVAGWTREQAEFGAKR
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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