SitesBLAST
Comparing RR42_RS05210 RR42_RS05210 malic enzyme 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)
P76558 NADP-dependent malic enzyme; NADP-ME; EC 1.1.1.40 from Escherichia coli (strain K12) (see paper)
64% identity, 97% coverage: 20:770/773 of query aligns to 4:755/759 of P76558
- K56 (≠ M72) modified: N6-acetyllysine
6zngF Maeb full-length acetyl-coa bound state (see paper)
46% identity, 97% coverage: 25:773/773 of query aligns to 8:747/753 of 6zngF
- active site: Y38 (= Y55), A74 (= A91), K93 (= K110), E135 (= E152), D136 (= D153), D160 (= D177), D161 (= D178), N286 (= N303)
- binding acetyl coenzyme *a: R511 (= R533), K514 (≠ D536), Y552 (≠ F575), A553 (≠ E576), R557 (≠ E580), L560 (≠ R583), P571 (≠ F595), T590 (≠ F614), V591 (= V615), N592 (= N616), L593 (≠ D617), Y625 (≠ H649), Q659 (= Q684), L690 (= L715), N694 (= N719), Q724 (≠ N750)
6zn4A Maeb malic enzyme domain apoprotein (see paper)
62% identity, 52% coverage: 25:423/773 of query aligns to 7:405/406 of 6zn4A
6zn7A Maeb malic enzyme domain apoprotein (see paper)
62% identity, 52% coverage: 25:423/773 of query aligns to 7:405/405 of 6zn7A
- active site: Y37 (= Y55), A73 (= A91), K92 (= K110), E134 (= E152), D135 (= D153), D159 (= D177), D160 (= D178), N285 (= N303)
- binding magnesium ion: E134 (= E152), D135 (= D153), D160 (= D178)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: T164 (= T182), N191 (≠ S209), A193 (= A211), G194 (= G212), A195 (= A213), S196 (≠ A214), D218 (= D236), S219 (= S237), K235 (= K253), L260 (≠ C278), S261 (= S279), V262 (≠ T280), M283 (≠ L301), N285 (= N303), V315 (= V333)
5ceeA Malic enzyme from candidatus phytoplasma aywb in complex with NAD and mg2+ (see paper)
48% identity, 49% coverage: 46:420/773 of query aligns to 25:385/387 of 5ceeA
- active site: Y34 (= Y55), A70 (= A91), K89 (= K110), E131 (= E152), D132 (= D153), D156 (= D177), D157 (= D178), N283 (= N303)
- binding magnesium ion: E131 (= E152), D132 (= D153), D157 (= D178)
- binding nicotinamide-adenine-dinucleotide: T161 (= T182), N188 (≠ S209), G189 (= G210), G191 (= G212), A193 (= A214), D213 (= D236), K214 (≠ S237), V258 (≠ C278), S259 (= S279), I263 (≠ V283), L281 (= L301), N283 (= N303), V312 (= V333), N314 (= N335)
2dvmA NAD complex structure of ph1275 protein from pyrococcus horikoshii
45% identity, 53% coverage: 21:426/773 of query aligns to 1:402/438 of 2dvmA
- active site: Y37 (= Y55), R73 (≠ A91), K92 (= K110), E134 (= E152), D135 (= D153), D159 (= D177), D160 (= D178), N296 (= N303)
- binding nicotinamide-adenine-dinucleotide: T164 (= T182), G194 (= G212), A195 (= A213), A196 (= A214), V217 (= V235), E218 (≠ D236), L219 (vs. gap), P224 (≠ G239), F269 (≠ C278), T270 (≠ S279), L294 (= L301), N296 (= N303), N327 (= N335)
2a9fA Crystal structure of a putative malic enzyme ((s)-malate:nad+ oxidoreductase (decarboxylating))
46% identity, 51% coverage: 20:411/773 of query aligns to 4:378/383 of 2a9fA
2haeD Crystal structure of a putative malic enzyme (malate oxidoreductase)
46% identity, 51% coverage: 25:415/773 of query aligns to 2:373/373 of 2haeD
2haeB Crystal structure of a putative malic enzyme (malate oxidoreductase)
46% identity, 51% coverage: 25:415/773 of query aligns to 2:373/373 of 2haeB
- active site: Y31 (= Y55), A67 (= A91), K86 (= K110), E128 (= E152), D129 (= D153), D153 (= D177), D154 (= D178), N280 (= N303)
- binding nicotinamide-adenine-dinucleotide: T158 (= T182), N185 (≠ S209), G188 (= G212), A189 (= A213), A190 (= A214), D210 (= D236), R211 (≠ S237), V255 (≠ C278), S256 (= S279), R257 (≠ T280), L278 (= L301), A279 (= A302), N280 (= N303), N311 (= N335)
Q8ZND6 Phosphate acetyltransferase; Phosphotransacetylase; EC 2.3.1.222; EC 2.3.1.8 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
29% identity, 44% coverage: 430:770/773 of query aligns to 390:710/714 of Q8ZND6
Sites not aligning to the query:
- 252 R→H: Increases speed of forward and back reactions by 2-3 fold. Not inhibited by NADH.
- 273 G→D: Increases speed of forward and back reactions by 2-3 fold.
- 294 M→I: Slightly decreases speed of forward and back reactions.
6ioxA Crystal structure of porphyromonas gingivalis phosphotransacetylase in complex with acetyl-coa (see paper)
32% identity, 43% coverage: 445:773/773 of query aligns to 7:338/339 of 6ioxA
1xcoD Crystal structure of a phosphotransacetylase from bacillus subtilis in complex with acetylphosphate (see paper)
27% identity, 40% coverage: 459:769/773 of query aligns to 20:324/325 of 1xcoD
P16243 NADP-dependent malic enzyme, chloroplastic; NADP-ME; EC 1.1.1.40 from Zea mays (Maize) (see 3 papers)
27% identity, 49% coverage: 51:431/773 of query aligns to 180:622/636 of P16243
- R237 (≠ A91) mutation to L: Decreases kcat 530-fold. Increases Km for NADP 36-fold and Km for malate 10-fold.
- K255 (= K110) mutation to I: Increases Km for malate 10-fold, and Km for NADP 15-fold. Decreases kcat 200-fold.
- E339 (= E163) mutation to A: No effect on kcat and Km for NADP. Increases Km for malate 2-fold.
- A387 (= A214) mutation to G: Decreases kcat 48-fold. Increases Km for NADP 4-fold. Increases Km for malate 6-fold.
- A392 (≠ L219) mutation to G: No effect on kcat. Increases Km for NADP 3.5-fold. Increases Km for malate 2.5-fold.
- KK 435:436 (≠ KA 253:254) mutation to LL: No effect on kcat and on Km for malate. Increases Km for NADP 9-fold.
- Q503 (≠ K314) mutation to E: No effect on kcat and Km for NADP. Increases Km for malate 2-fold.
- L544 (≠ I342) mutation to F: No effect on kcat and Km for NADP. Increases Km for malate 2-fold.
Sites not aligning to the query:
- 140 F→I: Decreases kcat 8-fold. Decreases Km for NADP 2-fold, increases Km for malate 2-fold.
2af3C Phosphotransacetylase from methanosarcina thermophila soaked with coenzyme a (see paper)
26% identity, 41% coverage: 453:771/773 of query aligns to 11:329/332 of 2af3C
- binding coenzyme a: R86 (= R533), S127 (≠ F575), L131 (= L579), V135 (≠ R583), L146 (≠ V594), A147 (≠ F595), G172 (≠ F614), M173 (≠ V615), M173 (≠ V615), V174 (≠ N616), E175 (≠ D617), N278 (= N719), Y281 (≠ F722), K282 (≠ N723), Q285 (≠ K726), G294 (= G736), P295 (= P737), T297 (≠ L739), D306 (≠ I748), L307 (= L749), S308 (≠ N750)
P38503 Phosphate acetyltransferase; Phosphotransacetylase; EC 2.3.1.8 from Methanosarcina thermophila (see 2 papers)
26% identity, 41% coverage: 453:771/773 of query aligns to 12:330/333 of P38503
- C159 (vs. gap) mutation to A: Loss of activity.; mutation to S: No loss of activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1gq2A Malic enzyme from pigeon liver (see paper)
26% identity, 51% coverage: 48:441/773 of query aligns to 83:538/555 of 1gq2A
- active site: Y90 (= Y55), R143 (≠ A91), K161 (= K110), E233 (= E152), D234 (= D153), D256 (= D177), D257 (= D178), N396 (= N303)
- binding manganese (ii) ion: K161 (= K110), E233 (= E152), D234 (= D153), D257 (= D178)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R143 (≠ A91), G146 (= G94), N237 (≠ A156), T261 (= T182), G289 (= G210), A290 (= A211), G291 (= G212), E292 (≠ A213), A293 (= A214), V322 (= V235), D323 (= D236), S324 (= S237), A368 (≠ S279), I370 (vs. gap), L394 (= L301), N396 (= N303), G440 (≠ V333), N441 (= N334), N442 (= N335)
- binding oxalate ion: R143 (≠ A91), L145 (= L93), D257 (= D178), N396 (= N303), N442 (= N335)
P40927 NADP-dependent malic enzyme; NADP-ME; EC 1.1.1.40 from Columba livia (Rock dove) (see 3 papers)
26% identity, 51% coverage: 48:441/773 of query aligns to 84:539/557 of P40927
- D141 (≠ N88) mutation to N: Increases Km for manganese 14-fold. Increases Km for malate 5-fold.
- R144 (≠ A91) binding ; binding
- K162 (= K110) binding ; mutation to A: Decreases kcat 235-fold. no effect on Km for NADP.
- D194 (= D131) mutation to N: No effect on Km for manganese. Increases Km for malate 8-fold.
- E234 (= E152) binding
- D235 (= D153) binding
- N238 (≠ A156) binding
- D258 (= D178) binding
- AGEA 291:294 (≠ AGAA 211:214) binding
- S325 (= S237) binding
- K340 (= K253) mutation to A: Increases Km for NADP 65-fold. No effect on kcat.
- N397 (= N303) binding
- N443 (= N335) binding ; binding
- D464 (≠ E356) mutation to N: No effect.
6c7nB Monoclinic form of malic enzyme from sorghum at 2 angstroms resolution (see paper)
28% identity, 49% coverage: 51:431/773 of query aligns to 97:539/553 of 6c7nB
- active site: Y101 (= Y55), R154 (≠ A91), K172 (= K110), E244 (= E152), D245 (= D153), D267 (= D177), D268 (= D178), L348 (≠ M249), N409 (= N303)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R154 (≠ A91), L156 (= L93), G157 (= G94), N248 (≠ A156), T272 (= T182), L299 (≠ S209), G300 (= G210), A301 (= A211), G302 (= G212), E303 (≠ A213), A304 (= A214), D335 (= D236), S336 (= S237), K352 (= K253), T380 (≠ C278), S381 (= S279), L407 (= L301), S408 (≠ A302), N409 (= N303), S452 (≠ V333), N454 (= N335)
- binding pyruvic acid: Y101 (= Y55), R154 (≠ A91), L156 (= L93)
Sites not aligning to the query:
6c7nA Monoclinic form of malic enzyme from sorghum at 2 angstroms resolution (see paper)
28% identity, 49% coverage: 51:431/773 of query aligns to 97:539/553 of 6c7nA
- active site: Y101 (= Y55), R154 (≠ A91), K172 (= K110), E244 (= E152), D245 (= D153), D267 (= D177), D268 (= D178), L348 (≠ M249), N409 (= N303)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: T272 (= T182), L299 (≠ S209), G300 (= G210), A301 (= A211), G302 (= G212), E303 (≠ A213), A304 (= A214), D335 (= D236), S336 (= S237), K352 (= K253), T380 (≠ C278), S381 (= S279), L407 (= L301), S408 (≠ A302), N409 (= N303), S452 (≠ V333)
Sites not aligning to the query:
6w29A Trypanosoma cruzi malic enzyme in complex with inhibitor (mec013) (see paper)
26% identity, 42% coverage: 51:374/773 of query aligns to 84:491/545 of 6w29A
Query Sequence
>RR42_RS05210 RR42_RS05210 malic enzyme
MTSKTGGDAPQHAPNSPEAQLRLAALEYHRSPTKGKIQVNATKALSNQRDLSLAYSPGVA
YACEEIAKDPAMAAEYTSRGNLVAVITNGTAVLGMGDIGPLAGKPVMEGKGCLFKKFAGI
DVFDIELDAHDPDKIVEIVAALEPTIGGVNLEDIKAPECFYIEKKLRERMNIPVFHDDQH
GTAIISGAALLNGLKVVGKDIAKVKLAVSGAGAAAIACLDTMVSLGVTRSNVSVVDSKGV
IYVGRDANMEPNKARYAQDTSNRTLADIVNGADVFLGCSTAGVLTAEMVKTMADKPIILA
LANPEPEIRPEVAKAARPDCIIATGRSDYPNQVNNVLCFPYIFRGALDCGATKITEAMKL
ACVKAIADLAEAELNDAVAAAYGGQELKFGPDYIIPTPFDQRLIEKIAPAVAKAAEESGV
ATRPIKDLEAYRQQLTQYVYHTGLIMKPVFTAAKAAPKRVVYAEGEEERVLRAVQTVVDE
GLARPILIGRPHVIQMRIDKAGLRLKAGADFELINPEDDPRYRAYHEAYHTLRGRDGVTP
DVAKVMLRRSNTLIGTMLMHMGDADAMLCGTVGRFEAHLEHVRDVIGMAPGAKVFAAMNA
LMLEKYTLFITDTFVNDDPTAEELAAITQLAAEEIARFGQHPKVALMSHSMFGSSDRPSA
RKMRAAQEILAREAPHLEVEGEMQGDAALVEDVRRHFLPGTKLAGSANLLVMPTLDAANI
AFNLLKITGGQGVTIGPILLGAAKPVHILNPQATTRRIVNMTAVAVAEANAVR
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