SitesBLAST
Comparing GFF2998 FitnessBrowser__Phaeo:GFF2998 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
4gfiC Crystal structure of efi-502318, an enolase family member from agrobacterium tumefaciens with homology to dipeptide epimerases (bound sodium, l-ala-l-glu with ordered loop)
57% identity, 99% coverage: 3:321/321 of query aligns to 5:327/327 of 4gfiC
- active site: F18 (= F16), T125 (= T119), K148 (= K142), K150 (= K144), D175 (= D169), L199 (= L193), E201 (= E195), C222 (= C216), D224 (= D218), K246 (= K240), C274 (= C268), D296 (= D290)
- binding alanine: K150 (= K144), C274 (= C268), D296 (= D290), D298 (= D292)
- binding glutamic acid: F18 (= F16), R25 (= R23), Y49 (= Y47), K150 (= K144), D175 (= D169), D224 (= D218), K246 (= K240), C274 (= C268)
3ijqA Structure of dipeptide epimerase from bacteroides thetaiotaomicron complexed with l-ala-d-glu; productive substrate binding. (see paper)
36% identity, 94% coverage: 1:301/321 of query aligns to 1:314/337 of 3ijqA
- active site: F16 (= F16), T129 (= T119), L152 (= L141), K153 (= K142), K155 (= K144), D179 (= D169), N181 (= N171), E206 (= E195), D231 (= D218), E232 (= E219), K253 (= K240), G280 (= G267), C281 (= C268), M282 (= M269), D300 (≠ V287), A302 (≠ T289), D303 (= D290), L304 (= L291)
- binding alanine: D303 (= D290), D305 (= D292)
- binding d-glutamic acid: F16 (= F16), R23 (= R23), P47 (≠ Y47), Y49 (≠ R49), K253 (= K240), M282 (= M269)
- binding magnesium ion: D179 (= D169), E206 (= E195), D231 (= D218)
Q8A861 L-Ala-D/L-Glu epimerase; AE epimerase; AEE; EC 5.1.1.20 from Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) (see paper)
36% identity, 94% coverage: 1:301/321 of query aligns to 46:359/383 of Q8A861
- D224 (= D169) binding
- E251 (= E195) binding
- D276 (= D218) binding
3ijlA Structure of dipeptide epimerase from bacteroides thetaiotaomicron complexed with l-pro-d-glu; nonproductive substrate binding. (see paper)
36% identity, 93% coverage: 2:301/321 of query aligns to 1:313/336 of 3ijlA
- active site: F15 (= F16), T128 (= T119), L151 (= L141), K152 (= K142), K154 (= K144), D178 (= D169), N180 (= N171), E205 (= E195), D230 (= D218), E231 (= E219), K252 (= K240), G279 (= G267), C280 (= C268), M281 (= M269), D299 (≠ V287), A301 (≠ T289), D302 (= D290), L303 (= L291)
- binding d-glutamic acid: F15 (= F16), V17 (≠ I18), R22 (= R23), P46 (≠ Y47), Y48 (≠ R49), K252 (= K240), C280 (= C268), M281 (= M269)
- binding magnesium ion: D178 (= D169), E205 (= E195), D230 (= D218)
- binding proline: C280 (= C268), D302 (= D290), D304 (= D292), L308 (= L296)
3q4dA Crystal structure of dipeptide epimerase from cytophaga hutchinsonii complexed with mg and dipeptide d-ala-l-ala (see paper)
30% identity, 93% coverage: 2:300/321 of query aligns to 5:328/368 of 3q4dA
- active site: F19 (= F16), P50 (= P46), T53 (≠ R49), T135 (= T119), K160 (= K142), K162 (= K144), D190 (= D169), N192 (= N171), E216 (= E195), D241 (= D218), E242 (= E219), S243 (= S220), K265 (= K240), G292 (= G267), G293 (≠ C268), F294 (≠ M269), Y317 (≠ T289), D318 (= D290), F319 (≠ L291)
- binding alanine: K162 (= K144), K265 (= K240), G293 (≠ C268)
- binding d-alanine: F19 (= F16), K162 (= K144), G293 (≠ C268), D318 (= D290), D320 (= D292), T321 (≠ G293)
- binding magnesium ion: D190 (= D169), E216 (= E195), D241 (= D218)
3q45A Crystal structure of dipeptide epimerase from cytophaga hutchinsonii complexed with mg and dipeptide d-ala-l-val (see paper)
30% identity, 93% coverage: 2:300/321 of query aligns to 5:328/368 of 3q45A
- active site: F19 (= F16), P50 (= P46), T53 (≠ R49), T135 (= T119), K160 (= K142), K162 (= K144), D190 (= D169), N192 (= N171), E216 (= E195), D241 (= D218), E242 (= E219), S243 (= S220), K265 (= K240), G292 (= G267), G293 (≠ C268), F294 (≠ M269), Y317 (≠ T289), D318 (= D290), F319 (≠ L291)
- binding d-alanine: F19 (= F16), K162 (= K144), D318 (= D290), D320 (= D292), T321 (≠ G293)
- binding magnesium ion: D190 (= D169), E216 (= E195), D241 (= D218)
- binding valine: K160 (= K142), K162 (= K144), D190 (= D169), K265 (= K240), G293 (≠ C268), F294 (≠ M269)
1tkkA The structure of a substrate-liganded complex of the l-ala-d/l-glu epimerase from bacillus subtilis (see paper)
32% identity, 90% coverage: 12:300/321 of query aligns to 15:331/359 of 1tkkA
- active site: F19 (= F16), P50 (= P46), V53 (≠ A48), T135 (= T119), K160 (= K142), K162 (= K144), L190 (≠ V168), D191 (= D169), A192 (= A170), N193 (= N171), E219 (= E195), D244 (= D218), E245 (= E219), S246 (= S220), N266 (= N238), K268 (= K240), G295 (= G267), S296 (≠ C268), M297 (= M269), F320 (vs. gap), D321 (= D290), F322 (≠ L291)
- binding alanine: K160 (= K142), K162 (= K144), D321 (= D290), D323 (= D292)
- binding glutamic acid: F19 (= F16), R24 (≠ G21), K160 (= K142), D191 (= D169), K268 (= K240), S296 (≠ C268), M297 (= M269), I298 (≠ V270)
- binding magnesium ion: D191 (= D169), E219 (= E195), D244 (= D218)
1jpmA L-ala-d/l-glu epimerase (see paper)
32% identity, 90% coverage: 12:300/321 of query aligns to 15:331/359 of 1jpmA
- active site: F19 (= F16), P50 (= P46), V53 (≠ A48), T135 (= T119), K160 (= K142), K162 (= K144), L190 (≠ V168), D191 (= D169), A192 (= A170), N193 (= N171), E219 (= E195), D244 (= D218), E245 (= E219), S246 (= S220), N266 (= N238), K268 (= K240), G295 (= G267), S296 (≠ C268), M297 (= M269), F320 (vs. gap), D321 (= D290), F322 (≠ L291)
- binding magnesium ion: D191 (= D169), E219 (= E195), D244 (= D218)
O34508 L-Ala-D/L-Glu epimerase; AE epimerase; AEE; EC 5.1.1.20 from Bacillus subtilis (strain 168) (see 2 papers)
32% identity, 90% coverage: 12:300/321 of query aligns to 15:331/366 of O34508
- R24 (≠ G21) binding
- T135 (= T119) binding
- K160 (= K142) binding
- K162 (= K144) active site, Proton acceptor; specific for (R)-substrate epimerization
- D191 (= D169) binding
- E219 (= E195) binding
- D244 (= D218) binding
- K268 (= K240) active site, Proton acceptor; specific for (S)-substrate epimerization
- S296 (≠ C268) binding
- I298 (≠ V270) binding
- D321 (= D290) binding
- D323 (= D292) binding
3kumA Crystal structure of dipeptide epimerase from enterococcus faecalis v583 complexed with mg and dipeptide l-arg-l-tyr (see paper)
33% identity, 83% coverage: 2:269/321 of query aligns to 5:293/354 of 3kumA
- active site: F19 (= F16), P50 (= P46), F53 (≠ A48), T134 (= T119), K159 (= K142), K161 (= K144), D189 (= D169), N191 (= N171), E215 (= E195), D240 (= D218), E241 (= E219), S242 (= S220), N262 (= N238), K264 (= K240), G291 (= G267), C292 (= C268), M293 (= M269)
- binding arginine: F19 (= F16), K161 (= K144), C292 (= C268)
- binding magnesium ion: D189 (= D169), E215 (= E195), D240 (= D218)
- binding tyrosine: I21 (= I18), F53 (≠ A48), I54 (≠ R49), K161 (= K144), D240 (= D218), K264 (= K240)
Sites not aligning to the query:
3k1gA Crystal structure of dipeptide epimerase from enterococcus faecalis v583 complexed with mg and dipeptide l-ser-l-tyr (see paper)
33% identity, 83% coverage: 2:269/321 of query aligns to 5:293/354 of 3k1gA
- active site: F19 (= F16), P50 (= P46), F53 (≠ A48), T134 (= T119), K159 (= K142), K161 (= K144), D189 (= D169), N191 (= N171), E215 (= E195), D240 (= D218), E241 (= E219), S242 (= S220), N262 (= N238), K264 (= K240), G291 (= G267), C292 (= C268), M293 (= M269)
- binding magnesium ion: D189 (= D169), E215 (= E195), D240 (= D218)
- binding serine: F19 (= F16), K161 (= K144), C292 (= C268)
- binding tyrosine: I21 (= I18), F53 (≠ A48), K161 (= K144), D189 (= D169), D240 (= D218), K264 (= K240), C292 (= C268)
Sites not aligning to the query:
3jvaB Crystal structure of dipeptide epimerase from enterococcus faecalis v583 (see paper)
33% identity, 83% coverage: 2:269/321 of query aligns to 5:293/354 of 3jvaB
- active site: F19 (= F16), P50 (= P46), F53 (≠ A48), T134 (= T119), K159 (= K142), K161 (= K144), D189 (= D169), N191 (= N171), E215 (= E195), D240 (= D218), E241 (= E219), S242 (= S220), N262 (= N238), K264 (= K240), G291 (= G267), C292 (= C268), M293 (= M269)
- binding magnesium ion: D189 (= D169), E215 (= E195), D240 (= D218)
Sites not aligning to the query:
3jzuA Crystal structure of dipeptide epimerase from enterococcus faecalis v583 complexed with mg and dipeptide l-leu-l-tyr (see paper)
33% identity, 83% coverage: 2:269/321 of query aligns to 5:293/353 of 3jzuA
- active site: F19 (= F16), P50 (= P46), F53 (≠ A48), T134 (= T119), K159 (= K142), K161 (= K144), D189 (= D169), N191 (= N171), E215 (= E195), D240 (= D218), E241 (= E219), S242 (= S220), N262 (= N238), K264 (= K240), G291 (= G267), C292 (= C268), M293 (= M269)
- binding leucine: K161 (= K144), C292 (= C268)
- binding magnesium ion: D189 (= D169), E215 (= E195), D240 (= D218)
- binding tyrosine: I21 (= I18), I26 (≠ R23), F53 (≠ A48), K161 (= K144), N191 (= N171), D240 (= D218), K264 (= K240), M293 (= M269)
Sites not aligning to the query:
3jw7A Crystal structure of dipeptide epimerase from enterococcus faecalis v583 complexed with mg and dipeptide l-ile-l-tyr (see paper)
33% identity, 83% coverage: 2:269/321 of query aligns to 5:293/353 of 3jw7A
- active site: F19 (= F16), P50 (= P46), F53 (≠ A48), T134 (= T119), K159 (= K142), K161 (= K144), D189 (= D169), N191 (= N171), E215 (= E195), D240 (= D218), E241 (= E219), S242 (= S220), N262 (= N238), K264 (= K240), G291 (= G267), C292 (= C268), M293 (= M269)
- binding isoleucine: K161 (= K144), C292 (= C268)
- binding magnesium ion: D189 (= D169), E215 (= E195), D240 (= D218)
- binding tyrosine: F53 (≠ A48), I54 (≠ R49), K161 (= K144), D240 (= D218), K264 (= K240), C292 (= C268)
Sites not aligning to the query:
2p8cA Crystal structure of n-succinyl arg/lys racemase from bacillus cereus atcc 14579 complexed with n-succinyl arg. (see paper)
31% identity, 89% coverage: 16:300/321 of query aligns to 19:330/369 of 2p8cA
- active site: F19 (= F16), A50 (= A48), H53 (≠ G51), V136 (≠ T119), F160 (≠ L141), K161 (= K142), M162 (≠ I143), K163 (= K144), D191 (= D169), N193 (= N171), E218 (= E195), D243 (= D218), E244 (= E219), G245 (vs. gap), N265 (= N238), K267 (= K240), G294 (= G267), S295 (≠ C268), M296 (= M269), V319 (vs. gap), E320 (≠ D290), L321 (= L291)
- binding magnesium ion: D191 (= D169), E218 (= E195), D243 (= D218)
- binding n~2~-(3-carboxypropanoyl)-l-arginine: F19 (= F16), Y26 (≠ R23), M29 (≠ A26), D51 (≠ R49), K163 (= K144), D191 (= D169), D243 (= D218), K267 (= K240), S295 (≠ C268), M296 (= M269), E320 (≠ D290), L321 (= L291), T322 (≠ D292)
2p8bA Crystal structure of n-succinyl arg/lys racemase from bacillus cereus atcc 14579 complexed with n-succinyl lys. (see paper)
31% identity, 89% coverage: 16:300/321 of query aligns to 19:330/369 of 2p8bA
- active site: F19 (= F16), A50 (= A48), H53 (≠ G51), V136 (≠ T119), F160 (≠ L141), K161 (= K142), M162 (≠ I143), K163 (= K144), D191 (= D169), N193 (= N171), E218 (= E195), D243 (= D218), E244 (= E219), G245 (vs. gap), N265 (= N238), K267 (= K240), G294 (= G267), S295 (≠ C268), M296 (= M269), V319 (vs. gap), E320 (≠ D290), L321 (= L291)
- binding magnesium ion: D191 (= D169), E218 (= E195), D243 (= D218)
- binding n-succinyl lysine: F19 (= F16), Y26 (≠ R23), D51 (≠ R49), V136 (≠ T119), K161 (= K142), K163 (= K144), D243 (= D218), K267 (= K240), S295 (≠ C268), M296 (= M269), E320 (≠ D290), L321 (= L291), T322 (≠ D292)
2p88A Crystal structure of n-succinyl arg/lys racemase from bacillus cereus atcc 14579 (see paper)
31% identity, 89% coverage: 16:300/321 of query aligns to 19:330/369 of 2p88A
- active site: F19 (= F16), A50 (= A48), H53 (≠ G51), V136 (≠ T119), F160 (≠ L141), K161 (= K142), M162 (≠ I143), K163 (= K144), D191 (= D169), N193 (= N171), E218 (= E195), D243 (= D218), E244 (= E219), G245 (vs. gap), N265 (= N238), K267 (= K240), G294 (= G267), S295 (≠ C268), M296 (= M269), V319 (vs. gap), E320 (≠ D290), L321 (= L291)
- binding magnesium ion: D191 (= D169), E218 (= E195), D243 (= D218)
Q81IL5 N-succinyl-L-Arg/Lys racemase; N-succinyl amino acid racemase; NSAR; EC 5.1.1.- from Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711) (see paper)
31% identity, 89% coverage: 16:300/321 of query aligns to 19:330/369 of Q81IL5
- D191 (= D169) binding
- E218 (= E195) binding
- D243 (= D218) binding
3desA Crystal structure of dipeptide epimerase from thermotoga maritima complexed with l-ala-l-phe dipeptide (see paper)
27% identity, 93% coverage: 1:300/321 of query aligns to 3:325/341 of 3desA
- active site: F18 (= F16), T132 (= T119), K157 (= K142), K159 (= K144), D186 (= D169), E214 (= E195), D239 (= D218), E240 (= E219), S241 (= S220), K263 (= K240), G289 (= G267), C290 (= C268), M291 (= M269), H314 (≠ T289), D315 (= D290), L316 (= L291)
- binding alanine: K159 (= K144), C290 (= C268), D315 (= D290), D317 (= D292)
- binding magnesium ion: D186 (= D169), E214 (= E195), D239 (= D218)
- binding phenylalanine: K159 (= K144), D186 (= D169), D239 (= D218), K263 (= K240), C290 (= C268), M291 (= M269)
3derA Crystal structure of dipeptide epimerase from thermotoga maritima complexed with l-ala-l-lys dipeptide (see paper)
27% identity, 93% coverage: 1:300/321 of query aligns to 3:325/341 of 3derA
- active site: F18 (= F16), T132 (= T119), K157 (= K142), K159 (= K144), D186 (= D169), E214 (= E195), D239 (= D218), E240 (= E219), S241 (= S220), K263 (= K240), G289 (= G267), C290 (= C268), M291 (= M269), H314 (≠ T289), D315 (= D290), L316 (= L291)
- binding alanine: K159 (= K144), C290 (= C268), D315 (= D290), D317 (= D292)
- binding lysine: F18 (= F16), K159 (= K144), D186 (= D169), K263 (= K240), C290 (= C268)
- binding magnesium ion: D186 (= D169), E214 (= E195), D239 (= D218)
Query Sequence
>GFF2998 FitnessBrowser__Phaeo:GFF2998
MQISVTPDTFKLAQVFTISRGSRTEAKVLTVRIIQDGVTGCGECVPYARYGETLESVTAE
IEGLPETFNRAELQSLLPAGAARNAVDCALWDLEAKQAGKRVWELAGLPEPKPEITAYTL
SLDSPENMQAQAAKNAHRPLLKIKLGTADDMARLEAVRAGAPEARIIVDANEGWSAEVYA
DLAPHLVRLGVDLVEQPLPAGEDAALLGMERPVPVCADESCHDRESLAALEGKYDVINIK
LDKTGGLTEALKLRDAALAQGFEVMVGCMVGSSLAMAPATLVAQGAVVTDLDGPLLLAED
REEPLDFDADGVHPPKAALWG
Or try a new SitesBLAST search
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