SitesBLAST
Comparing BWI76_RS03435 FitnessBrowser__Koxy:BWI76_RS03435 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)
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)
33% identity, 97% coverage: 8:362/367 of query aligns to 1:355/361 of Q9RKF7
- D195 (= D199) binding
- E221 (= E225) binding
- E247 (= E251) binding
3ck5A Crystal structure of a racemase from streptomyces coelicolor a3(2) with bound magnesium
33% identity, 97% coverage: 8:362/367 of query aligns to 1:352/357 of 3ck5A
- active site: T19 (≠ W26), T50 (= T57), G137 (≠ S142), K164 (= K169), K166 (= K171), D195 (= D199), N197 (= N201), I220 (= I224), E221 (= E225), I243 (= I247), G246 (= G250), E247 (= E251), E268 (≠ Q272), D270 (= D274), H297 (= H301), G298 (≠ F302), V299 (= V303), Y315 (= Y319), E317 (= E321)
- binding magnesium ion: D195 (= D199), E221 (= E225), E247 (= E251)
2pp1A Crystal structure of l-talarate/galactarate dehydratase from salmonella typhimurium lt2 liganded with mg and l-lyxarohydroxamate (see paper)
34% identity, 89% coverage: 33:357/367 of query aligns to 54:377/395 of 2pp1A
- active site: S78 (≠ T57), K192 (= K169), K194 (= K171), D223 (= D199), N225 (= N201), E249 (= E225), G274 (= G250), E275 (= E251), D298 (= D274), H325 (= H301), E345 (= E321)
- binding (2r,3s,4r)-2,3,4-trihydroxy-5-(hydroxyamino)-5-oxopentanoic acid: K79 (≠ S58), F168 (≠ N145), K194 (= K171), E275 (= E251), H325 (= H301), E345 (= E321)
- binding magnesium ion: D223 (= D199), E249 (= E225), E275 (= E251)
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)
34% identity, 89% coverage: 33:357/367 of query aligns to 57:380/398 of Q8ZL58
- KR 82:83 (≠ SG 58:59) binding
- K195 (= K169) binding
- K197 (= K171) active site, Proton acceptor; mutation to A: Loss of dehydration activity on both L-talarate and galactarate and loss of epimerization activity.
- D226 (= D199) binding
- N228 (= N201) binding
- E252 (= E225) binding
- E278 (= E251) binding
- H328 (= H301) 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 (= E321) binding
Sites not aligning to the query:
2og9A Crystal structure of mandelate racemase/muconate lactonizing enzyme from polaromonas sp. Js666
35% identity, 89% coverage: 33:357/367 of query aligns to 22:345/363 of 2og9A
- active site: S46 (≠ T57), T132 (vs. gap), K160 (= K169), K162 (= K171), D191 (= D199), N193 (= N201), E217 (= E225), G242 (= G250), E243 (= E251), M264 (≠ Q272), D266 (= D274), H293 (= H301), F294 (= F302), A295 (≠ V303), E313 (= E321)
- binding calcium ion: A232 (≠ R240), F235 (≠ S243)
3cb3A Crystal structure of l-talarate dehydratase from polaromonas sp. Js666 complexed with mg and l-glucarate
35% identity, 89% coverage: 33:357/367 of query aligns to 33:356/373 of 3cb3A
- active site: S57 (≠ T57), T143 (vs. gap), K171 (= K169), K173 (= K171), D202 (= D199), N204 (= N201), E228 (= E225), G253 (= G250), E254 (= E251), M275 (≠ Q272), D277 (= D274), H304 (= H301), F305 (= F302), A306 (≠ V303), E324 (= E321)
- binding l-glucaric acid: K171 (= K169), K173 (= K171), D202 (= D199), E254 (= E251), H304 (= H301)
- binding magnesium ion: D202 (= D199), E228 (= E225), A243 (≠ R240), F246 (≠ S243), E254 (= E251)
Sites not aligning to the query:
2pp3A Crystal structure of l-talarate/galactarate dehydratase mutant k197a liganded with mg and l-glucarate (see paper)
34% identity, 89% coverage: 33:357/367 of query aligns to 54:377/395 of 2pp3A
- active site: S78 (≠ T57), K192 (= K169), A194 (≠ K171), D223 (= D199), N225 (= N201), E249 (= E225), G274 (= G250), E275 (= E251), D298 (= D274), H325 (= H301), E345 (= E321)
- binding l-glucaric acid: K79 (≠ S58), K192 (= K169), D223 (= D199), N225 (= N201), E275 (= E251), H325 (= H301), E345 (= E321), F347 (≠ T323)
- binding magnesium ion: D223 (= D199), E249 (= E225), E275 (= E251)
Sites not aligning to the query:
5xd8B Crystal structure analysis of 3,6-anhydro-l-galactonate cycloisomerase (see paper)
33% identity, 60% coverage: 93:312/367 of query aligns to 91:311/367 of 5xd8B
- active site: G140 (≠ S142), K167 (= K169), K169 (= K171), D198 (= D199), N200 (= N201), E224 (= E225), G249 (= G250), E250 (= E251), Q271 (= Q272), D273 (= D274), H300 (= H301), G301 (≠ F302), M302 (≠ V303)
- binding magnesium ion: D198 (= D199), E224 (= E225), E250 (= E251)
Sites not aligning to the query:
4h19A Crystal structure of an enolase (mandelate racemase subgroup, target efi-502087) from agrobacterium tumefaciens, with bound mg and d- ribonohydroxamate, ordered loop
33% identity, 80% coverage: 9:301/367 of query aligns to 3:305/372 of 4h19A
- active site: I20 (≠ W26), T51 (= T57), T143 (≠ S142), K172 (= K169), K174 (= K171), D203 (= D199), N205 (= N201), E229 (= E225), G254 (= G250), E255 (= E251), Q276 (= Q272), D278 (= D274), H305 (= H301)
- binding (2R,3R,4R)-N,2,3,4,5-pentakis(oxidanyl)pentanamide: D22 (= D28), H25 (= H31), H52 (≠ S58), K172 (= K169), K174 (= K171), D203 (= D199), N205 (= N201), E229 (= E225), E255 (= E251), H305 (= H301)
- binding calcium ion: D268 (≠ E264), H298 (= H294)
- binding magnesium ion: D203 (= D199), E229 (= E225), E255 (= E251)
Sites not aligning to the query:
3ugvF Crystal structure of an enolase from alpha pretobacterium bal199 (efi target efi-501650) with bound mg
28% identity, 92% coverage: 29:367/367 of query aligns to 23:363/364 of 3ugvF
- active site: P51 (≠ T57), P54 (≠ G62), A95 (= A100), S137 (= S142), K168 (= K169), R170 (≠ K171), D199 (= D199), N201 (= N201), E225 (= E225), G250 (= G250), E251 (= E251), N252 (= N252), M272 (≠ Q272), D274 (= D274), A293 (= A293), H301 (= H301), L302 (≠ F302), Y303 (≠ V303), E321 (= E321)
- binding magnesium ion: D199 (= D199), E225 (= E225), R240 (= R240), L243 (≠ S243), E251 (= E251)
Sites not aligning to the query:
3tteA Crystal structure of enolase brado_4202 (target efi-501651) from bradyrhizobium complexed with magnesium and mandelic acid
29% identity, 90% coverage: 38:367/367 of query aligns to 35:360/361 of 3tteA
- active site: A54 (≠ S55), R57 (≠ S58), Q98 (≠ A100), S140 (= S142), K166 (= K169), K168 (= K171), D197 (= D199), N199 (= N201), E223 (= E225), G248 (= G250), E249 (= E251), N250 (= N252), M270 (≠ Q272), D272 (= D274), I294 (≠ L296), H299 (= H301), I300 (≠ F302), L301 (≠ V303), H316 (≠ S318), E319 (= E321)
- binding magnesium ion: D197 (= D199), E223 (= E225), E249 (= E251)
- binding (s)-mandelic acid: K166 (= K169), D197 (= D199), N199 (= N201), E223 (= E225), E249 (= E251), H299 (= H301), E319 (= E321)
Sites not aligning to the query:
3toyA Crystal structure of enolase brado_4202 (target efi-501651) from bradyrhizobium sp. Ors278 with calcium and acetate bound
29% identity, 90% coverage: 38:367/367 of query aligns to 33:358/359 of 3toyA
- active site: A52 (≠ S55), R55 (≠ S58), Q96 (≠ A100), S138 (= S142), K164 (= K169), K166 (= K171), D195 (= D199), N197 (= N201), E221 (= E225), G246 (= G250), E247 (= E251), N248 (= N252), M268 (≠ Q272), D270 (= D274), I292 (≠ L296), H297 (= H301), I298 (≠ F302), L299 (≠ V303), H314 (≠ S318), E317 (= E321)
- binding calcium ion: D195 (= D199), E221 (= E225), R236 (= R240), S239 (= S243), E247 (= E251)
Sites not aligning to the query:
P11444 Mandelate racemase; MR; EC 5.1.2.2 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 3 papers)
29% identity, 87% coverage: 38:356/367 of query aligns to 34:348/359 of P11444
- K166 (= K171) mutation K->A,M,Q: Loss of activity.
- D195 (= D199) binding
- E221 (= E225) binding
- E247 (= E251) binding
- H297 (= H301) mutation to N: Loss of activity.
- E317 (= E321) binding ; mutation to Q: Reduces activity 10000-fold.
7mqxE P. Putida mandelate racemase forms an oxobenzoxaborole adduct with 2- formylphenylboronic acid (see paper)
29% identity, 87% coverage: 38:356/367 of query aligns to 33:347/358 of 7mqxE
Sites not aligning to the query:
6vimA P. Putida mandelate racemase co-crystallized with phenylboronic acid (see paper)
29% identity, 87% coverage: 38:356/367 of query aligns to 32:346/357 of 6vimA
- active site: S137 (= S142), K162 (= K169), K164 (= K171), D193 (= D199), N195 (= N201), E219 (= E225), G244 (= G250), E245 (= E251), D268 (= D274), H295 (= H301), L296 (≠ F302), F297 (≠ V303), E315 (= E321)
- binding magnesium ion: D193 (= D199), E219 (= E225), E245 (= E251)
- binding phenyl boronic acid: K162 (= K169), K164 (= K171), D193 (= D199), E245 (= E251), H295 (= H301), L296 (≠ F302), E315 (= E321), L317 (≠ T323)
Sites not aligning to the query:
4x2pA P. Putida mandelate racemase in complex with 3-hydroxypyruvate (see paper)
29% identity, 87% coverage: 38:356/367 of query aligns to 32:346/357 of 4x2pA
- active site: S137 (= S142), K162 (= K169), K164 (= K171), D193 (= D199), N195 (= N201), E219 (= E225), G244 (= G250), E245 (= E251), D268 (= D274), M292 (= M298), H295 (= H301), L296 (≠ F302), F297 (≠ V303), A311 (≠ I317), E315 (= E321)
- binding 3-hydroxypyruvic acid: K162 (= K169), K164 (= K171), D193 (= D199), H295 (= H301), E315 (= E321)
- binding magnesium ion: D193 (= D199), E219 (= E225), E245 (= E251)
Sites not aligning to the query:
4m6uA P. Putida mandelate racemase co-crystallized with tartronic acid (see paper)
29% identity, 87% coverage: 38:356/367 of query aligns to 32:346/357 of 4m6uA
- active site: S137 (= S142), K162 (= K169), K164 (= K171), D193 (= D199), N195 (= N201), E219 (= E225), G244 (= G250), E245 (= E251), D268 (= D274), M292 (= M298), H295 (= H301), L296 (≠ F302), F297 (≠ V303), A311 (≠ I317), E315 (= E321)
- binding magnesium ion: D193 (= D199), E219 (= E225), E245 (= E251)
- binding tartronate: K162 (= K169), K164 (= K171), D193 (= D199), E245 (= E251), H295 (= H301), E315 (= E321)
Sites not aligning to the query:
4fp1A P. Putida mandelate racemase co-crystallized with 3,3,3-trifluoro-2- hydroxy-2-(trifluoromethyl) propionic acid (see paper)
29% identity, 87% coverage: 38:356/367 of query aligns to 32:346/357 of 4fp1A
- active site: S137 (= S142), K162 (= K169), K164 (= K171), D193 (= D199), N195 (= N201), E219 (= E225), G244 (= G250), E245 (= E251), D268 (= D274), M292 (= M298), H295 (= H301), L296 (≠ F302), F297 (≠ V303), A311 (≠ I317), E315 (= E321)
- binding 3,3,3-trifluoro-2-hydroxy-2-(trifluoromethyl)propanoic acid: K164 (= K171), H295 (= H301), L296 (≠ F302)
- binding magnesium ion: D193 (= D199), E219 (= E225), E245 (= E251)
Sites not aligning to the query:
3uxlA P. Putida mandelate racemase co-crystallized with the intermediate analogue cupferron (see paper)
29% identity, 87% coverage: 38:356/367 of query aligns to 32:346/357 of 3uxlA
- active site: S137 (= S142), K162 (= K169), K164 (= K171), D193 (= D199), N195 (= N201), E219 (= E225), G244 (= G250), E245 (= E251), D268 (= D274), M292 (= M298), H295 (= H301), L296 (≠ F302), F297 (≠ V303), A311 (≠ I317), E315 (= E321)
- binding 1-hydroxy-2-oxo-1-phenylhydrazine: K162 (= K169), K164 (= K171), D193 (= D199), N195 (= N201), E245 (= E251), H295 (= H301)
- binding magnesium ion: D193 (= D199), E219 (= E225), E245 (= E251)
Sites not aligning to the query:
3uxkA P. Putida mandelate racemase co-crystallized with the intermediate analogue benzohydroxamate (see paper)
29% identity, 87% coverage: 38:356/367 of query aligns to 32:346/357 of 3uxkA
- active site: S137 (= S142), K162 (= K169), K164 (= K171), D193 (= D199), N195 (= N201), E219 (= E225), G244 (= G250), E245 (= E251), D268 (= D274), M292 (= M298), H295 (= H301), L296 (≠ F302), F297 (≠ V303), A311 (≠ I317), E315 (= E321)
- binding benzhydroxamic acid: K162 (= K169), K164 (= K171), D193 (= D199), N195 (= N201), E245 (= E251), H295 (= H301), L317 (≠ T323)
- binding magnesium ion: D193 (= D199), E219 (= E225), E245 (= E251)
Sites not aligning to the query:
Query Sequence
>BWI76_RS03435 FitnessBrowser__Koxy:BWI76_RS03435
MNSTKMPVIENIELMTARVPLPEGPWGDQIHHVTDIEVAIVDVYGSNGHVGTGFSHTSGW
CGKTISALIAEIIPDVIGQPLSPRGLWHRSYKHVHDVGGAGVTTHALAALDIAYWDLLGK
TLNAPIIDILGRVRDRVPLYGSGINLHLSIEEVIDQVKRWKSTGYLAAKVKVGKPTLEED
VERLRKIQEAVPGFPLAVDANQGWNFPQALRAFKLFEPLNLLWIEEPMPSDDIAGHLRLR
ERSATPIALGENVYNLNQFTQYIESGSADYIQADLGRVGGITGYLDIAAVARAHNLPMTP
HFVMELSASLLATVPNISYAEMTDGGRWKDLRIIAEAGEEVDGYYVPSERPGHGIILDRD
YLATHKI
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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