SitesBLAST
Comparing N515DRAFT_2182 N515DRAFT_2182 malate dehydrogenase (oxaloacetate-decarboxylating)(NADP+) 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)
59% identity, 99% coverage: 5:755/761 of query aligns to 3:757/759 of P76558
- K56 (≠ A58) modified: N6-acetyllysine
6zngF Maeb full-length acetyl-coa bound state (see paper)
45% identity, 99% coverage: 11:761/761 of query aligns to 8:753/753 of 6zngF
- active site: Y38 (= Y41), A74 (= A77), K93 (= K96), E135 (= E138), D136 (= D139), D160 (= D163), D161 (= D164), N286 (= N288)
- binding acetyl coenzyme *a: R511 (≠ T517), K514 (≠ R520), Y552 (≠ F559), A553 (≠ H560), R557 (≠ G564), L560 (≠ R567), P571 (≠ T579), T590 (≠ H598), V591 (= V599), N592 (≠ Q600), L593 (≠ V601), Y625 (≠ H633), Q659 (= Q668), L690 (= L699), N694 (= N703), Q724 (≠ T733)
6zn4A Maeb malic enzyme domain apoprotein (see paper)
59% identity, 52% coverage: 11:407/761 of query aligns to 7:405/406 of 6zn4A
6zn7A Maeb malic enzyme domain apoprotein (see paper)
59% identity, 52% coverage: 11:407/761 of query aligns to 7:405/405 of 6zn7A
- active site: Y37 (= Y41), A73 (= A77), K92 (= K96), E134 (= E138), D135 (= D139), D159 (= D163), D160 (= D164), N285 (= N288)
- binding magnesium ion: E134 (= E138), D135 (= D139), D160 (= D164)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: T164 (= T168), N191 (≠ A195), A193 (= A197), G194 (= G198), A195 (= A199), S196 (≠ A200), D218 (= D222), S219 (≠ R223), K235 (= K238), L260 (= L263), S261 (= S264), V262 (≠ A265), M283 (≠ L286), N285 (= N288), V315 (= V318)
5ceeA Malic enzyme from candidatus phytoplasma aywb in complex with NAD and mg2+ (see paper)
46% identity, 48% coverage: 36:404/761 of query aligns to 29:385/387 of 5ceeA
- active site: Y34 (= Y41), A70 (= A77), K89 (= K96), E131 (= E138), D132 (= D139), D156 (= D163), D157 (= D164), N283 (= N288)
- binding magnesium ion: E131 (= E138), D132 (= D139), D157 (= D164)
- binding nicotinamide-adenine-dinucleotide: T161 (= T168), N188 (≠ A195), G189 (= G196), G191 (= G198), A193 (= A200), D213 (= D222), K214 (≠ R223), V258 (≠ L263), S259 (= S264), I263 (≠ V268), L281 (= L286), N283 (= N288), V312 (= V318), N314 (= N320)
2dvmA NAD complex structure of ph1275 protein from pyrococcus horikoshii
41% identity, 58% coverage: 7:448/761 of query aligns to 1:433/438 of 2dvmA
- active site: Y37 (= Y41), R73 (≠ A77), K92 (= K96), E134 (= E138), D135 (= D139), D159 (= D163), D160 (= D164), N296 (= N288)
- binding nicotinamide-adenine-dinucleotide: T164 (= T168), G194 (= G198), A195 (= A199), A196 (= A200), V217 (vs. gap), E218 (vs. gap), L219 (= L219), P224 (≠ E224), F269 (≠ L263), T270 (≠ S264), L294 (= L286), N296 (= N288), N327 (= N320)
2a9fA Crystal structure of a putative malic enzyme ((s)-malate:nad+ oxidoreductase (decarboxylating))
47% identity, 44% coverage: 21:354/761 of query aligns to 18:350/383 of 2a9fA
2haeD Crystal structure of a putative malic enzyme (malate oxidoreductase)
45% identity, 51% coverage: 11:399/761 of query aligns to 2:373/373 of 2haeD
2haeB Crystal structure of a putative malic enzyme (malate oxidoreductase)
45% identity, 51% coverage: 11:399/761 of query aligns to 2:373/373 of 2haeB
- active site: Y31 (= Y41), A67 (= A77), K86 (= K96), E128 (= E138), D129 (= D139), D153 (= D163), D154 (= D164), N280 (= N288)
- binding nicotinamide-adenine-dinucleotide: T158 (= T168), N185 (≠ A195), G188 (= G198), A189 (= A199), A190 (= A200), D210 (= D222), R211 (= R223), V255 (≠ L263), S256 (= S264), R257 (≠ A265), L278 (= L286), A279 (= A287), N280 (= N288), N311 (= N320)
1xcoD Crystal structure of a phosphotransacetylase from bacillus subtilis in complex with acetylphosphate (see paper)
28% identity, 43% coverage: 429:752/761 of query aligns to 6:324/325 of 1xcoD
Q8ZND6 Phosphate acetyltransferase; Phosphotransacetylase; EC 2.3.1.222; EC 2.3.1.8 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
28% identity, 45% coverage: 415:757/761 of query aligns to 372:714/714 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)
28% identity, 43% coverage: 429:752/761 of query aligns to 7:334/339 of 6ioxA
2af3C Phosphotransacetylase from methanosarcina thermophila soaked with coenzyme a (see paper)
24% identity, 43% coverage: 429:752/761 of query aligns to 3:327/332 of 2af3C
- binding coenzyme a: R86 (≠ T517), S127 (≠ F559), L131 (= L563), V135 (≠ R567), L146 (≠ C578), A147 (≠ T579), G172 (≠ H598), M173 (≠ V599), M173 (≠ V599), V174 (≠ Q600), E175 (≠ V601), N278 (= N703), Y281 (= Y706), K282 (≠ N707), Q285 (≠ R710), G294 (= G719), P295 (= P720), T297 (≠ L722), D306 (≠ I731), L307 (= L732), S308 (≠ T733)
P38503 Phosphate acetyltransferase; Phosphotransacetylase; EC 2.3.1.8 from Methanosarcina thermophila (see 2 papers)
24% identity, 43% coverage: 429:752/761 of query aligns to 4:328/333 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
Q9SIU0 NAD-dependent malic enzyme 1, mitochondrial; AtNAD-ME1; NAD-malic enzyme 1; EC 1.1.1.39 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
28% identity, 43% coverage: 23:352/761 of query aligns to 141:542/623 of Q9SIU0
Sites not aligning to the query:
- 122 R→A: Impaired fumarate-mediated allosteric activation.
P40927 NADP-dependent malic enzyme; NADP-ME; EC 1.1.1.40 from Columba livia (Rock dove) (see 3 papers)
24% identity, 42% coverage: 34:353/761 of query aligns to 84:476/557 of P40927
- D141 (≠ N74) mutation to N: Increases Km for manganese 14-fold. Increases Km for malate 5-fold.
- R144 (≠ A77) binding ; binding
- K162 (= K96) binding ; mutation to A: Decreases kcat 235-fold. no effect on Km for NADP.
- D194 (= D117) mutation to N: No effect on Km for manganese. Increases Km for malate 8-fold.
- E234 (= E138) binding
- D235 (= D139) binding
- N238 (≠ A142) binding
- D258 (= D164) binding
- AGEA 291:294 (≠ AGAA 197:200) binding
- S325 (≠ R223) binding
- K340 (= K238) mutation to A: Increases Km for NADP 65-fold. No effect on kcat.
- N397 (= N288) binding
- N443 (= N320) binding ; binding
- D464 (≠ E341) mutation to N: No effect.
1gq2A Malic enzyme from pigeon liver (see paper)
24% identity, 42% coverage: 34:353/761 of query aligns to 83:475/555 of 1gq2A
- active site: Y90 (= Y41), R143 (≠ A77), K161 (= K96), E233 (= E138), D234 (= D139), D256 (= D163), D257 (= D164), N396 (= N288)
- binding manganese (ii) ion: K161 (= K96), E233 (= E138), D234 (= D139), D257 (= D164)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R143 (≠ A77), G146 (= G80), N237 (≠ A142), T261 (= T168), G289 (= G196), A290 (= A197), G291 (= G198), E292 (≠ A199), A293 (= A200), V322 (≠ Y221), D323 (= D222), S324 (≠ R223), A368 (≠ S264), I370 (vs. gap), L394 (= L286), N396 (= N288), G440 (≠ V318), N441 (= N319), N442 (= N320)
- binding oxalate ion: R143 (≠ A77), L145 (= L79), D257 (= D164), N396 (= N288), N442 (= N320)
8eyoA Crystal structure of human mitochondrial NADP+ malic enzyme 3 with NADP bound (see paper)
25% identity, 42% coverage: 34:353/761 of query aligns to 82:474/562 of 8eyoA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: T260 (= T168), Q287 (≠ A195), A289 (= A197), G290 (= G198), E291 (≠ A199), A292 (= A200), D322 (= D222), S323 (≠ R223), K338 (= K238), V366 (≠ L263), A367 (≠ S264), I369 (vs. gap), L393 (= L286), S394 (≠ A287), N395 (= N288), G439 (≠ V318), N441 (= N320)
P16243 NADP-dependent malic enzyme, chloroplastic; NADP-ME; EC 1.1.1.40 from Zea mays (Maize) (see 3 papers)
25% identity, 53% coverage: 37:438/761 of query aligns to 180:636/636 of P16243
- R237 (≠ A77) mutation to L: Decreases kcat 530-fold. Increases Km for NADP 36-fold and Km for malate 10-fold.
- K255 (= K96) mutation to I: Increases Km for malate 10-fold, and Km for NADP 15-fold. Decreases kcat 200-fold.
- E339 (= E149) mutation to A: No effect on kcat and Km for NADP. Increases Km for malate 2-fold.
- A387 (= A200) mutation to G: Decreases kcat 48-fold. Increases Km for NADP 4-fold. Increases Km for malate 6-fold.
- A392 (≠ L205) mutation to G: No effect on kcat. Increases Km for NADP 3.5-fold. Increases Km for malate 2.5-fold.
- KK 435:436 (≠ KQ 238:239) mutation to LL: No effect on kcat and on Km for malate. Increases Km for NADP 9-fold.
- Q503 (≠ D297) mutation to E: No effect on kcat and Km for NADP. Increases Km for malate 2-fold.
- L544 (≠ I327) 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.
6w49A Trypanosoma cruzi malic enzyme in complex with inhibitor (mec010) (see paper)
27% identity, 36% coverage: 69:343/761 of query aligns to 131:467/543 of 6w49A
Sites not aligning to the query:
Query Sequence
>N515DRAFT_2182 N515DRAFT_2182 malate dehydrogenase (oxaloacetate-decarboxylating)(NADP+)
MALPEELRLAALEYHRLPRPGKIKVSATKAMVTQRDLSLAYSPGVAYACEAIVEDANAAS
EMTARGNLVAVITNGTAVLGLGDIGPLAGKPVMEGKGVLFQKFAGIDVFDIEIDERDPDK
LVDIIASLEPTFGGINLEDIKAPECFIVERKLRERMKIPVFHDDQHGTAIIVGAAVLNAL
EVVGKKIEDVKLATAGAGAAGIACLDMLVALGLKPEHILAYDREGVLYTGRDHMDPDKQR
YARDTKARTLAEIVDGADIFLGLSAGGVLKPEMVATMGRQPIILALANPNPEILPEDAQR
VRPDCIIATGRSDYPNQVNNALCFPYIFRGALDVGATGINEAMKTACVRAIAQLARMEAG
DLASAYGGDVPTFGPDYLIPRPFDPRLLVMLAPAVAQAAMDSGVATRPITDMDAYKEKLG
QFIYRTGLLMKPVYERARADRKRVVYAEGEEETVLRAVQTVIDERLAFPILIGRPSVIET
RIQRLGLRMKEGVDFELTNIDDDPRFNDYWQQYHALTERRGVSPAAAKNLLRSRPTLIAS
LMVERGEADAMICGLVGRFHKKLGYMRSVFGLDPGVQCTSAMTGVINDQGAWFFLDTHVQ
VDPSAEQIAEATLQASYRLKLFGIEPKVALLSHSNYGSHDNPSAAKMRKVYELLKSRLPK
LEMDGEMQADTAWDEGLRTRMFPNTTLTGRANLFVMPNLDAANITYNMVRVMTDGVAIGP
ILMGIDKPAHILTPASTPRRVVNMTAIAAVDAQIRGQQKSR
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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