SitesBLAST
Comparing SMc00169 SMc00169 malic enzyme 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)
P76558 NADP-dependent malic enzyme; NADP-ME; EC 1.1.1.40 from Escherichia coli (strain K12) (see paper)
60% identity, 97% coverage: 18:767/770 of query aligns to 5:755/759 of P76558
- K56 (≠ T69) modified: N6-acetyllysine
6zngF Maeb full-length acetyl-coa bound state (see paper)
46% identity, 98% coverage: 17:768/770 of query aligns to 3:745/753 of 6zngF
- active site: Y38 (= Y52), A74 (= A88), K93 (= K107), E135 (= E149), D136 (= D150), D160 (= D174), D161 (= D175), N286 (= N300)
- binding acetyl coenzyme *a: R511 (≠ V531), K514 (≠ L534), Y552 (= Y573), A553 (≠ S574), R557 (= R578), L560 (≠ S581), P571 (≠ L591), T590 (≠ Y612), V591 (= V613), N592 (≠ S614), L593 (≠ F615), Y625 (≠ H647), Q659 (≠ H682), L690 (= L713), N694 (= N717), Q724 (≠ S747)
6zn4A Maeb malic enzyme domain apoprotein (see paper)
60% identity, 52% coverage: 17:420/770 of query aligns to 2:405/406 of 6zn4A
6zn7A Maeb malic enzyme domain apoprotein (see paper)
60% identity, 52% coverage: 17:420/770 of query aligns to 2:405/405 of 6zn7A
- active site: Y37 (= Y52), A73 (= A88), K92 (= K107), E134 (= E149), D135 (= D150), D159 (= D174), D160 (= D175), N285 (= N300)
- binding magnesium ion: E134 (= E149), D135 (= D150), D160 (= D175)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: T164 (= T179), N191 (≠ S206), A193 (= A208), G194 (= G209), A195 (= A210), S196 (≠ A211), D218 (= D233), S219 (≠ I234), K235 (= K250), L260 (= L275), S261 (= S276), V262 (≠ A277), M283 (≠ L298), N285 (= N300), V315 (= V330)
5ceeA Malic enzyme from candidatus phytoplasma aywb in complex with NAD and mg2+ (see paper)
46% identity, 49% coverage: 44:417/770 of query aligns to 26:385/387 of 5ceeA
- active site: Y34 (= Y52), A70 (= A88), K89 (= K107), E131 (= E149), D132 (= D150), D156 (= D174), D157 (= D175), N283 (= N300)
- binding magnesium ion: E131 (= E149), D132 (= D150), D157 (= D175)
- binding nicotinamide-adenine-dinucleotide: T161 (= T179), N188 (≠ S206), G189 (= G207), G191 (= G209), A193 (= A211), D213 (= D233), K214 (≠ I234), V258 (≠ L275), S259 (= S276), I263 (≠ V280), L281 (= L298), N283 (= N300), V312 (= V330), N314 (= N332)
2a9fA Crystal structure of a putative malic enzyme ((s)-malate:nad+ oxidoreductase (decarboxylating))
51% identity, 44% coverage: 32:366/770 of query aligns to 18:350/383 of 2a9fA
2dvmA NAD complex structure of ph1275 protein from pyrococcus horikoshii
43% identity, 53% coverage: 18:423/770 of query aligns to 1:402/438 of 2dvmA
- active site: Y37 (= Y52), R73 (≠ A88), K92 (= K107), E134 (= E149), D135 (= D150), D159 (= D174), D160 (= D175), N296 (= N300)
- binding nicotinamide-adenine-dinucleotide: T164 (= T179), G194 (= G209), A195 (= A210), A196 (= A211), V217 (vs. gap), E218 (vs. gap), L219 (vs. gap), P224 (vs. gap), F269 (≠ L275), T270 (≠ S276), L294 (= L298), N296 (= N300), N327 (= N332)
2haeD Crystal structure of a putative malic enzyme (malate oxidoreductase)
43% identity, 51% coverage: 22:412/770 of query aligns to 2:373/373 of 2haeD
2haeB Crystal structure of a putative malic enzyme (malate oxidoreductase)
43% identity, 51% coverage: 22:412/770 of query aligns to 2:373/373 of 2haeB
- active site: Y31 (= Y52), A67 (= A88), K86 (= K107), E128 (= E149), D129 (= D150), D153 (= D174), D154 (= D175), N280 (= N300)
- binding nicotinamide-adenine-dinucleotide: T158 (= T179), N185 (≠ S206), G188 (= G209), A189 (= A210), A190 (= A211), D210 (= D233), R211 (≠ I234), V255 (≠ L275), S256 (= S276), R257 (≠ A277), L278 (= L298), A279 (= A299), N280 (= N300), N311 (= N332)
6ioxA Crystal structure of porphyromonas gingivalis phosphotransacetylase in complex with acetyl-coa (see paper)
33% identity, 40% coverage: 455:761/770 of query aligns to 19:329/339 of 6ioxA
1xcoD Crystal structure of a phosphotransacetylase from bacillus subtilis in complex with acetylphosphate (see paper)
28% identity, 40% coverage: 457:766/770 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)
27% identity, 44% coverage: 428:768/770 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.
P38503 Phosphate acetyltransferase; Phosphotransacetylase; EC 2.3.1.8 from Methanosarcina thermophila (see 2 papers)
27% identity, 41% coverage: 456:767/770 of query aligns to 16:329/333 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
2af3C Phosphotransacetylase from methanosarcina thermophila soaked with coenzyme a (see paper)
27% identity, 41% coverage: 456:767/770 of query aligns to 15:328/332 of 2af3C
- binding coenzyme a: R86 (≠ V531), S127 (≠ Y573), L131 (= L577), V135 (≠ S581), L146 (≠ D592), A147 (≠ F593), G172 (≠ Y612), M173 (≠ V613), M173 (≠ V613), V174 (≠ S614), E175 (≠ F615), N278 (= N717), Y281 (≠ L720), K282 (≠ G721), Q285 (≠ K724), G294 (= G733), P295 (= P734), T297 (≠ L736), D306 (≠ I745), L307 (= L746), S308 (= S747)
P16243 NADP-dependent malic enzyme, chloroplastic; NADP-ME; EC 1.1.1.40 from Zea mays (Maize) (see 3 papers)
25% identity, 49% coverage: 48:428/770 of query aligns to 180:622/636 of P16243
- R237 (≠ A88) mutation to L: Decreases kcat 530-fold. Increases Km for NADP 36-fold and Km for malate 10-fold.
- K255 (= K107) mutation to I: Increases Km for malate 10-fold, and Km for NADP 15-fold. Decreases kcat 200-fold.
- E339 (= E160) mutation to A: No effect on kcat and Km for NADP. Increases Km for malate 2-fold.
- A387 (= A211) mutation to G: Decreases kcat 48-fold. Increases Km for NADP 4-fold. Increases Km for malate 6-fold.
- A392 (≠ L216) 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 250:251) mutation to LL: No effect on kcat and on Km for malate. Increases Km for NADP 9-fold.
- Q503 (≠ V309) mutation to E: No effect on kcat and Km for NADP. Increases Km for malate 2-fold.
- L544 (≠ I339) 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)
24% identity, 50% coverage: 45:429/770 of query aligns to 83:528/555 of 1gq2A
- active site: Y90 (= Y52), R143 (≠ A88), K161 (= K107), E233 (= E149), D234 (= D150), D256 (= D174), D257 (= D175), N396 (= N300)
- binding manganese (ii) ion: K161 (= K107), E233 (= E149), D234 (= D150), D257 (= D175)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R143 (≠ A88), G146 (= G91), N237 (≠ A153), T261 (= T179), G289 (= G207), A290 (= A208), G291 (= G209), E292 (≠ A210), A293 (= A211), V322 (≠ H232), D323 (= D233), S324 (≠ I234), A368 (≠ S276), I370 (vs. gap), L394 (= L298), N396 (= N300), G440 (≠ V330), N441 (= N331), N442 (= N332)
- binding oxalate ion: R143 (≠ A88), L145 (= L90), D257 (= D175), N396 (= N300), N442 (= N332)
P40927 NADP-dependent malic enzyme; NADP-ME; EC 1.1.1.40 from Columba livia (Rock dove) (see 3 papers)
24% identity, 50% coverage: 45:429/770 of query aligns to 84:529/557 of P40927
- D141 (≠ N85) mutation to N: Increases Km for manganese 14-fold. Increases Km for malate 5-fold.
- R144 (≠ A88) binding ; binding
- K162 (= K107) binding ; mutation to A: Decreases kcat 235-fold. no effect on Km for NADP.
- D194 (vs. gap) mutation to N: No effect on Km for manganese. Increases Km for malate 8-fold.
- E234 (= E149) binding
- D235 (= D150) binding
- N238 (≠ A153) binding
- D258 (= D175) binding
- AGEA 291:294 (≠ AGAA 208:211) binding
- S325 (≠ I234) binding
- K340 (≠ W249) mutation to A: Increases Km for NADP 65-fold. No effect on kcat.
- N397 (= N300) binding
- N443 (= N332) binding ; binding
- D464 (≠ E353) mutation to N: No effect.
1gz3A Molecular mechanism for the regulation of human mitochondrial NAD(p)+- dependent malic enzyme by atp and fumarate (see paper)
27% identity, 38% coverage: 82:370/770 of query aligns to 140:486/554 of 1gz3A
- active site: R146 (≠ A88), K164 (= K107), E236 (= E149), D237 (= D150), D259 (= D174), D260 (= D175), N402 (= N300)
- binding adenosine-5'-triphosphate: R146 (≠ A88), N240 (≠ A153), A293 (= A208), G294 (= G209), E295 (≠ A210), A296 (= A211), D326 (= D233), K327 (≠ I234), V373 (≠ L275), A374 (≠ S276), G375 (≠ A277), L379 (≠ V280)
- binding manganese (ii) ion: E236 (= E149), D237 (= D150), D260 (= D175)
- binding oxalate ion: R146 (≠ A88), L148 (= L90), K164 (= K107), N402 (= N300), N448 (= N332)
Sites not aligning to the query:
7xdgA Cryo-em structures of human mitochondrial NAD(p)+-dependent malic enzyme in a ternary complex with NAD+ and allosteric inhibitor mdsa
27% identity, 38% coverage: 82:370/770 of query aligns to 137:483/551 of 7xdgA
- binding nicotinamide-adenine-dinucleotide: I171 (= I117), R172 (≠ D118), R175 (vs. gap), F241 (= F157), D257 (= D175), T261 (= T179), L288 (≠ S206), A290 (= A208), A293 (= A211), F322 (≠ H232), D323 (= D233), K324 (≠ I234), V370 (≠ L275), A371 (≠ S276), A373 (= A278), L376 (≠ V280), S398 (≠ A299), I457 (≠ L344), L458 (≠ D345)
Sites not aligning to the query:
7xdfA Cryo-em structures of human mitochondrial NAD(p)+-dependent malic enzyme in a ternary complex with NAD+ and allosteric inhibitor ea
27% identity, 38% coverage: 82:370/770 of query aligns to 137:483/551 of 7xdfA
- binding 4-[(3-carboxy-2-oxidanyl-naphthalen-1-yl)methyl]-3-oxidanyl-naphthalene-2-carboxylic acid: Y153 (≠ A99), M197 (vs. gap)
- binding nicotinamide-adenine-dinucleotide: I171 (= I117), R172 (≠ D118), R175 (vs. gap), F241 (= F157), D257 (= D175), T261 (= T179), A290 (= A208), A293 (= A211), D323 (= D233), K324 (≠ I234), V370 (≠ L275), A371 (≠ S276), G372 (≠ A277), S398 (≠ A299), N399 (= N300), L458 (≠ D345)
Sites not aligning to the query:
Query Sequence
>SMc00169 SMc00169 malic enzyme
MNTGDKAKSQAVPASGDIDQQALFFHRYPRPGKLEIQPTKPLGNQRDLALAYSPGVAAPC
LAIKDNPETAADFTARANLVAVVSNGTAVLGLGNIGPLASKPVMEGKAVLFKKFAGIDVF
DIEIDAPTVDRMVDVISALEPTFGGINLEDIKAPECFEVERRLREKMEIPVFHDDQHGTA
IIVAAAVLNGLELAGKDIAEAKIVASGAGAAALACLNLLVTLGARRENIWVHDIEGLVYK
GREALMDEWKAVYAQESDNRVLADSIGGADVFLGLSAAGVLKPELLARMAEKPLIMALAN
PTPEIMPEVARAARPDAMICTGRSDFPNQVNNVLCFPHIFRGALDCGARTINEEMKMAAV
RAIAGLAREEPSDVAARAYSGETPVFGPDYLIPSPFDQRLILRIAPAVAKAAAESGVATR
PIQDFDAYLDKLNRFVFRSGFIMKPVFAAAKNAAKNRVIFAEGEDERVLRAAQVLLEEGT
AKPILIGRPQIIETRLRRYGLRIRPDVDFEVVNPEGDPRYRDYVDDYFALVGRLGVIPEA
ARTIVRTNTTVIGALAVKRGEADALICGVEGRYSRHLRDVSQIIGKRSGVLDFSALSLLI
SQRGATFFTDTYVSFSPSAEEIAQTTVMAANEIRRFGITPRAALVSHSNFGSRDSESAFK
MRTALQLVRELAPDLEVDGEMHGDSAISEVLRQRVMPDSTLNGEANLLVFPNLDAANITL
GVVKTMTDSLHVGPILLGSALPAHILSPSVTSRGVVNMAALAVVESSHPV
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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