SitesBLAST
Comparing H281DRAFT_05846 H281DRAFT_05846 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)
63% identity, 99% coverage: 1:754/760 of query aligns to 1:755/759 of P76558
- K56 (≠ D56) modified: N6-acetyllysine
6zngF Maeb full-length acetyl-coa bound state (see paper)
48% identity, 99% coverage: 4:754/760 of query aligns to 3:744/753 of 6zngF
- active site: Y38 (= Y39), A74 (= A75), K93 (= K94), E135 (= E136), D136 (= D137), D160 (= D161), D161 (= D162), N286 (= N286)
- binding acetyl coenzyme *a: R511 (≠ G517), K514 (≠ E520), Y552 (= Y559), A553 (≠ H560), R557 (≠ K564), L560 (≠ E567), P571 (≠ Q577), T590 (≠ Y598), V591 (= V599), N592 (= N600), L593 (≠ E601), Y625 (≠ N633), Q659 (≠ H668), L690 (≠ V699), N694 (= N703), Q724 (≠ T734)
6zn4A Maeb malic enzyme domain apoprotein (see paper)
61% identity, 53% coverage: 4:407/760 of query aligns to 2:405/406 of 6zn4A
6zn7A Maeb malic enzyme domain apoprotein (see paper)
61% identity, 53% coverage: 4:407/760 of query aligns to 2:405/405 of 6zn7A
- active site: Y37 (= Y39), A73 (= A75), K92 (= K94), E134 (= E136), D135 (= D137), D159 (= D161), D160 (= D162), N285 (= N286)
- binding magnesium ion: E134 (= E136), D135 (= D137), D160 (= D162)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: T164 (= T166), N191 (≠ S193), A193 (= A195), G194 (= G196), A195 (= A197), S196 (≠ A198), D218 (= D220), S219 (= S221), K235 (= K236), L260 (≠ C261), S261 (= S262), V262 (≠ S263), M283 (≠ L284), N285 (= N286), V315 (= V316)
5ceeA Malic enzyme from candidatus phytoplasma aywb in complex with NAD and mg2+ (see paper)
47% identity, 49% coverage: 34:404/760 of query aligns to 29:385/387 of 5ceeA
- active site: Y34 (= Y39), A70 (= A75), K89 (= K94), E131 (= E136), D132 (= D137), D156 (= D161), D157 (= D162), N283 (= N286)
- binding magnesium ion: E131 (= E136), D132 (= D137), D157 (= D162)
- binding nicotinamide-adenine-dinucleotide: T161 (= T166), N188 (≠ S193), G189 (= G194), G191 (= G196), A193 (= A198), D213 (= D220), K214 (≠ S221), V258 (≠ C261), S259 (= S262), I263 (≠ V266), L281 (= L284), N283 (= N286), V312 (= V316), N314 (= N318)
2dvmA NAD complex structure of ph1275 protein from pyrococcus horikoshii
45% identity, 53% coverage: 5:410/760 of query aligns to 1:402/438 of 2dvmA
- active site: Y37 (= Y39), R73 (≠ A75), K92 (= K94), E134 (= E136), D135 (= D137), D159 (= D161), D160 (= D162), N296 (= N286)
- binding nicotinamide-adenine-dinucleotide: T164 (= T166), G194 (= G196), A195 (= A197), A196 (= A198), V217 (vs. gap), E218 (vs. gap), L219 (vs. gap), P224 (≠ G223), F269 (≠ C261), T270 (≠ S262), L294 (= L284), N296 (= N286), N327 (= N318)
2a9fA Crystal structure of a putative malic enzyme ((s)-malate:nad+ oxidoreductase (decarboxylating))
49% identity, 46% coverage: 1:352/760 of query aligns to 1:350/383 of 2a9fA
2haeD Crystal structure of a putative malic enzyme (malate oxidoreductase)
45% identity, 51% coverage: 9:399/760 of query aligns to 2:373/373 of 2haeD
2haeB Crystal structure of a putative malic enzyme (malate oxidoreductase)
45% identity, 51% coverage: 9:399/760 of query aligns to 2:373/373 of 2haeB
- active site: Y31 (= Y39), A67 (= A75), K86 (= K94), E128 (= E136), D129 (= D137), D153 (= D161), D154 (= D162), N280 (= N286)
- binding nicotinamide-adenine-dinucleotide: T158 (= T166), N185 (≠ S193), G188 (= G196), A189 (= A197), A190 (= A198), D210 (= D220), R211 (≠ S221), V255 (≠ C261), S256 (= S262), R257 (≠ S263), L278 (= L284), A279 (= A285), N280 (= N286), N311 (= N318)
6ioxA Crystal structure of porphyromonas gingivalis phosphotransacetylase in complex with acetyl-coa (see paper)
32% identity, 43% coverage: 429:753/760 of query aligns to 7:334/339 of 6ioxA
1xcoD Crystal structure of a phosphotransacetylase from bacillus subtilis in complex with acetylphosphate (see paper)
29% identity, 41% coverage: 443:753/760 of query aligns to 20:324/325 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)
29% identity, 45% coverage: 415:755/760 of query aligns to 372:711/714 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.
2af3C Phosphotransacetylase from methanosarcina thermophila soaked with coenzyme a (see paper)
29% identity, 42% coverage: 437:753/760 of query aligns to 11:327/332 of 2af3C
- binding coenzyme a: R86 (≠ G517), S127 (≠ Y559), L131 (= L563), V135 (≠ E567), L146 (≠ N578), A147 (≠ F579), G172 (≠ Y598), M173 (≠ V599), M173 (≠ V599), V174 (≠ N600), E175 (= E601), N278 (= N703), Y281 (= Y706), K282 (≠ N707), Q285 (≠ K710), G294 (= G720), P295 (= P721), T297 (≠ L723), D306 (≠ V732), L307 (= L733), S308 (≠ T734)
P38503 Phosphate acetyltransferase; Phosphotransacetylase; EC 2.3.1.8 from Methanosarcina thermophila (see 2 papers)
29% identity, 42% coverage: 437:753/760 of query aligns to 12:328/333 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
P16243 NADP-dependent malic enzyme, chloroplastic; NADP-ME; EC 1.1.1.40 from Zea mays (Maize) (see 3 papers)
28% identity, 51% coverage: 35:425/760 of query aligns to 180:633/636 of P16243
- R237 (≠ A75) mutation to L: Decreases kcat 530-fold. Increases Km for NADP 36-fold and Km for malate 10-fold.
- K255 (= K94) mutation to I: Increases Km for malate 10-fold, and Km for NADP 15-fold. Decreases kcat 200-fold.
- E339 (= E147) mutation to A: No effect on kcat and Km for NADP. Increases Km for malate 2-fold.
- A387 (= A198) mutation to G: Decreases kcat 48-fold. Increases Km for NADP 4-fold. Increases Km for malate 6-fold.
- A392 (≠ L203) mutation to G: No effect on kcat. Increases Km for NADP 3.5-fold. Increases Km for malate 2.5-fold.
- KK 435:436 (≠ KE 236:237) mutation to LL: No effect on kcat and on Km for malate. Increases Km for NADP 9-fold.
- Q503 (≠ E295) mutation to E: No effect on kcat and Km for NADP. Increases Km for malate 2-fold.
- L544 (≠ I325) 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.
1gq2A Malic enzyme from pigeon liver (see paper)
28% identity, 38% coverage: 69:358/760 of query aligns to 137:483/555 of 1gq2A
- active site: R143 (≠ A75), K161 (= K94), E233 (= E136), D234 (= D137), D256 (= D161), D257 (= D162), N396 (= N286)
- binding manganese (ii) ion: K161 (= K94), E233 (= E136), D234 (= D137), D257 (= D162)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R143 (≠ A75), G146 (= G78), N237 (≠ A140), T261 (= T166), G289 (= G194), A290 (= A195), G291 (= G196), E292 (≠ A197), A293 (= A198), V322 (= V219), D323 (= D220), S324 (= S221), A368 (≠ S262), I370 (vs. gap), L394 (= L284), N396 (= N286), G440 (≠ V316), N441 (= N317), N442 (= N318)
- binding oxalate ion: R143 (≠ A75), L145 (= L77), D257 (= D162), N396 (= N286), N442 (= N318)
Sites not aligning to the query:
P40927 NADP-dependent malic enzyme; NADP-ME; EC 1.1.1.40 from Columba livia (Rock dove) (see 3 papers)
28% identity, 38% coverage: 69:358/760 of query aligns to 138:484/557 of P40927
- D141 (≠ N72) mutation to N: Increases Km for manganese 14-fold. Increases Km for malate 5-fold.
- R144 (≠ A75) binding ; binding
- K162 (= K94) binding ; mutation to A: Decreases kcat 235-fold. no effect on Km for NADP.
- D194 (= D115) mutation to N: No effect on Km for manganese. Increases Km for malate 8-fold.
- E234 (= E136) binding
- D235 (= D137) binding
- N238 (≠ A140) binding
- D258 (= D162) binding
- AGEA 291:294 (≠ AGAA 195:198) binding
- S325 (= S221) binding
- K340 (= K236) mutation to A: Increases Km for NADP 65-fold. No effect on kcat.
- N397 (= N286) binding
- N443 (= N318) binding ; binding
- D464 (≠ E339) mutation to N: No effect.
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)
27% identity, 38% coverage: 69:357/760 of query aligns to 190:549/623 of Q9SIU0
Sites not aligning to the query:
- 122 R→A: Impaired fumarate-mediated allosteric activation.
7x11A Crystal structure of me1 in complex with NADPH (see paper)
28% identity, 39% coverage: 69:366/760 of query aligns to 144:495/564 of 7x11A
- binding 6-[(7-methyl-2-propyl-imidazo[4,5-b]pyridin-4-yl)methyl]-2-[2-(1H-1,2,3,4-tetrazol-5-yl)phenyl]-1,3-benzothiazole: N244 (≠ A140), F248 (= F144), I265 (≠ Q163), Q266 (≠ H164), L302 (≠ I200), G303 (≠ A201), H306 (≠ D204), E345 (≠ S235), D470 (≠ E339)
- binding manganese (ii) ion: E240 (= E136), D241 (= D137), D264 (= D162)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R150 (≠ A75), N244 (≠ A140), T268 (= T166), A297 (= A195), G298 (= G196), E299 (≠ A197), A300 (= A198), D330 (= D220), S331 (= S221), K332 (= K222), K346 (= K236), V374 (≠ A255), A375 (≠ D256), A376 (≠ V257), I377 (≠ F258), L401 (= L284), S402 (≠ A285), N403 (= N286), G447 (≠ V316)
8eyoA Crystal structure of human mitochondrial NADP+ malic enzyme 3 with NADP bound (see paper)
28% identity, 38% coverage: 69:355/760 of query aligns to 136:478/562 of 8eyoA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: T260 (= T166), Q287 (≠ S193), A289 (= A195), G290 (= G196), E291 (≠ A197), A292 (= A198), D322 (= D220), S323 (= S221), K338 (= K236), V366 (≠ C261), A367 (≠ S262), I369 (vs. gap), L393 (= L284), S394 (≠ A285), N395 (= N286), G439 (≠ V316), N441 (= N318)
Query Sequence
>H281DRAFT_05846 H281DRAFT_05846 malate dehydrogenase (oxaloacetate-decarboxylating)(NADP+)
MDEQLKQSALAYHQNPKPGKISVTPTKPLSNQLDLSLAYSPGVAAACMAIYDEPLDAQKY
TSRGNLVGVITNGTAVLGLGNIGPLAAKPVMEGKGCLFKKFAGIDVFDIELAESDPDKLV
EAIAMLEPTLGGINLEDIKAPECFYIEKKLRERMKIPVFHDDQHGTAIIASAAILNGLKV
VGKKLDEVKLVCSGAGAAAIACLDLLVNLGLSKQNILVVDSKGVIYEGRGNLDPSKERYA
ASTEARTLADAIRGADVFLGCSSAGVLKPEMVAEMGTQPLILALANPEPEIRPEEAKKVR
PDCIIATGRSDYPNQVNNVLCFPFIFRGALDVGATTITEEMKLACVRAIAELAEETDQGD
EVAKAYEGHSLEFGPEYLIPKPFDPRLIIKIAPAVAQAAMDSGVATRPIKDMDAYREELG
TTVYRTGMVMRPVFAAAKSEPARIVFAEGEDERVLRAAQFVLLEKIAKPILVGRPSVIEM
RLKKMGSKLRCGEDFEIVDPEDDPRYQQCWQAYHELGAREGVTPDVAKAAMRKFNTLIGA
ILVRLGEADGMICGMIGQYHTHLKFIEQVLGKADNVQNFAAMNLLMLPGRNLFICDTYVN
ETPTAEQLADMTMLASREIEKFGITPKVALLSNSNFGSAPSASSQRMATARKLIVERAPT
LEIDGEMHGDAALSEMVRKAAFPGTTLSGEANLLIMPNVEAANIAYNLLKMVGGDGVTVG
PFLLGAEKPVHVLTPAATVRRIINMTAVASANARKSVNSK
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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