SitesBLAST
Comparing WP_024891696.1 NCBI__GCF_000559025.1:WP_024891696.1 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)
61% identity, 99% coverage: 3:754/761 of query aligns to 2:757/759 of P76558
- K56 (≠ A57) modified: N6-acetyllysine
6zngF Maeb full-length acetyl-coa bound state (see paper)
46% identity, 99% coverage: 5:755/761 of query aligns to 3:747/753 of 6zngF
- active site: Y38 (= Y40), A74 (= A76), K93 (= K95), E135 (= E137), D136 (= D138), D160 (= D162), D161 (= D163), N286 (= N287)
- binding acetyl coenzyme *a: R511 (≠ T516), K514 (≠ R519), Y552 (= Y564), A553 (≠ I565), R557 (≠ F569), L560 (≠ E572), P571 (≠ M581), T590 (≠ H597), V591 (= V598), N592 (≠ Q599), L593 (≠ H600), Y625 (≠ H632), Q659 (≠ M667), L690 (= L698), N694 (= N702), Q724 (≠ T732)
6zn4A Maeb malic enzyme domain apoprotein (see paper)
60% identity, 53% coverage: 5:406/761 of query aligns to 2:405/406 of 6zn4A
6zn7A Maeb malic enzyme domain apoprotein (see paper)
60% identity, 53% coverage: 5:406/761 of query aligns to 2:405/405 of 6zn7A
- active site: Y37 (= Y40), A73 (= A76), K92 (= K95), E134 (= E137), D135 (= D138), D159 (= D162), D160 (= D163), N285 (= N287)
- binding magnesium ion: E134 (= E137), D135 (= D138), D160 (= D163)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: T164 (= T167), N191 (≠ A194), A193 (= A196), G194 (= G197), A195 (= A198), S196 (≠ A199), D218 (= D221), S219 (≠ R222), K235 (= K237), L260 (= L262), S261 (= S263), V262 (≠ A264), M283 (≠ L285), N285 (= N287), V315 (= V317)
5ceeA Malic enzyme from candidatus phytoplasma aywb in complex with NAD and mg2+ (see paper)
48% identity, 48% coverage: 35:403/761 of query aligns to 29:385/387 of 5ceeA
- active site: Y34 (= Y40), A70 (= A76), K89 (= K95), E131 (= E137), D132 (= D138), D156 (= D162), D157 (= D163), N283 (= N287)
- binding magnesium ion: E131 (= E137), D132 (= D138), D157 (= D163)
- binding nicotinamide-adenine-dinucleotide: T161 (= T167), N188 (≠ A194), G189 (= G195), G191 (= G197), A193 (= A199), D213 (= D221), K214 (≠ R222), V258 (≠ L262), S259 (= S263), I263 (≠ V267), L281 (= L285), N283 (= N287), V312 (= V317), N314 (= N319)
2dvmA NAD complex structure of ph1275 protein from pyrococcus horikoshii
45% identity, 52% coverage: 6:404/761 of query aligns to 1:397/438 of 2dvmA
- active site: Y37 (= Y40), R73 (≠ A76), K92 (= K95), E134 (= E137), D135 (= D138), D159 (= D162), D160 (= D163), N296 (= N287)
- binding nicotinamide-adenine-dinucleotide: T164 (= T167), G194 (= G197), A195 (= A198), A196 (= A199), V217 (= V220), E218 (≠ D221), L219 (vs. gap), P224 (≠ D223), F269 (≠ L262), T270 (≠ S263), L294 (= L285), N296 (= N287), N327 (= N319)
2a9fA Crystal structure of a putative malic enzyme ((s)-malate:nad+ oxidoreductase (decarboxylating))
45% identity, 49% coverage: 20:394/761 of query aligns to 18:378/383 of 2a9fA
2haeD Crystal structure of a putative malic enzyme (malate oxidoreductase)
44% identity, 51% coverage: 10:398/761 of query aligns to 2:373/373 of 2haeD
2haeB Crystal structure of a putative malic enzyme (malate oxidoreductase)
44% identity, 51% coverage: 10:398/761 of query aligns to 2:373/373 of 2haeB
- active site: Y31 (= Y40), A67 (= A76), K86 (= K95), E128 (= E137), D129 (= D138), D153 (= D162), D154 (= D163), N280 (= N287)
- binding nicotinamide-adenine-dinucleotide: T158 (= T167), N185 (≠ A194), G188 (= G197), A189 (= A198), A190 (= A199), D210 (= D221), R211 (= R222), V255 (≠ L262), S256 (= S263), R257 (≠ A264), L278 (= L285), A279 (= A286), N280 (= N287), N311 (= N319)
6ioxA Crystal structure of porphyromonas gingivalis phosphotransacetylase in complex with acetyl-coa (see paper)
29% identity, 42% coverage: 428:748/761 of query aligns to 7:331/339 of 6ioxA
1xcoD Crystal structure of a phosphotransacetylase from bacillus subtilis in complex with acetylphosphate (see paper)
28% identity, 43% coverage: 428:751/761 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)
27% identity, 42% coverage: 436:751/761 of query aligns to 399:709/714 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)
23% identity, 42% coverage: 429:751/761 of query aligns to 4:327/332 of 2af3C
- binding coenzyme a: R86 (≠ T516), S127 (≠ F558), L131 (= L562), V135 (≠ R566), L146 (≠ S577), A147 (≠ T578), G172 (≠ H597), M173 (≠ V598), M173 (≠ V598), V174 (≠ Q599), E175 (≠ H600), N278 (= N702), Y281 (= Y705), K282 (≠ N706), Q285 (≠ R709), G294 (= G718), P295 (= P719), T297 (≠ L721), D306 (≠ V730), L307 (≠ M731), S308 (≠ T732)
P38503 Phosphate acetyltransferase; Phosphotransacetylase; EC 2.3.1.8 from Methanosarcina thermophila (see 2 papers)
23% identity, 42% coverage: 429:751/761 of query aligns to 5:328/333 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
1gq2A Malic enzyme from pigeon liver (see paper)
26% identity, 44% coverage: 33:365/761 of query aligns to 83:488/555 of 1gq2A
- active site: Y90 (= Y40), R143 (≠ A76), K161 (= K95), E233 (= E137), D234 (= D138), D256 (= D162), D257 (= D163), N396 (= N287)
- binding manganese (ii) ion: K161 (= K95), E233 (= E137), D234 (= D138), D257 (= D163)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R143 (≠ A76), G146 (= G79), N237 (≠ A141), T261 (= T167), G289 (= G195), A290 (= A196), G291 (= G197), E292 (≠ A198), A293 (= A199), V322 (= V220), D323 (= D221), S324 (≠ R222), A368 (≠ S263), I370 (vs. gap), L394 (= L285), N396 (= N287), G440 (≠ V317), N441 (= N318), N442 (= N319)
- binding oxalate ion: R143 (≠ A76), L145 (= L78), D257 (= D163), N396 (= N287), N442 (= N319)
P40927 NADP-dependent malic enzyme; NADP-ME; EC 1.1.1.40 from Columba livia (Rock dove) (see 3 papers)
26% identity, 44% coverage: 33:365/761 of query aligns to 84:489/557 of P40927
- D141 (≠ N73) mutation to N: Increases Km for manganese 14-fold. Increases Km for malate 5-fold.
- R144 (≠ A76) binding NADP(+); binding substrate
- K162 (= K95) binding substrate; mutation to A: Decreases kcat 235-fold. no effect on Km for NADP.
- D194 (= D116) mutation to N: No effect on Km for manganese. Increases Km for malate 8-fold.
- E234 (= E137) binding Mn(2+)
- D235 (= D138) binding Mn(2+)
- N238 (≠ A141) binding NADP(+)
- D258 (= D163) binding Mn(2+)
- AGEA 291:294 (≠ AGAA 196:199) binding NADP(+)
- S325 (≠ R222) binding NADP(+)
- K340 (= K237) mutation to A: Increases Km for NADP 65-fold. No effect on kcat.
- N397 (= N287) binding NADP(+)
- N443 (= N319) binding NADP(+); binding substrate
- D464 (≠ E340) 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)
26% identity, 42% coverage: 38:357/761 of query aligns to 141:548/623 of Q9SIU0
Sites not aligning to the query:
- 122 R→A: Impaired fumarate-mediated allosteric activation.
P16243 NADP-dependent malic enzyme, chloroplastic; NADP-ME; EC 1.1.1.40 from Zea mays (Maize) (see 3 papers)
27% identity, 53% coverage: 36:437/761 of query aligns to 180:636/636 of P16243
- R237 (≠ A76) mutation to L: Decreases kcat 530-fold. Increases Km for NADP 36-fold and Km for malate 10-fold.
- K255 (= K95) mutation to I: Increases Km for malate 10-fold, and Km for NADP 15-fold. Decreases kcat 200-fold.
- E339 (= E148) mutation to A: No effect on kcat and Km for NADP. Increases Km for malate 2-fold.
- A387 (= A199) mutation to G: Decreases kcat 48-fold. Increases Km for NADP 4-fold. Increases Km for malate 6-fold.
- A392 (≠ L204) 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 237:238) mutation to LL: No effect on kcat and on Km for malate. Increases Km for NADP 9-fold.
- Q503 (≠ H296) mutation to E: No effect on kcat and Km for NADP. Increases Km for malate 2-fold.
- L544 (≠ I326) 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.
9e6mA Crystal structure of the g200r mutant from the maize chloroplastic photosynthetic NADP(+)-dependent malic enzyme
26% identity, 43% coverage: 36:365/761 of query aligns to 109:512/565 of 9e6mA
Sites not aligning to the query:
7x11A Crystal structure of me1 in complex with NADPH (see paper)
24% identity, 44% coverage: 33:365/761 of query aligns to 90:495/564 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 (≠ A141), F248 (= F145), I265 (≠ Q164), Q266 (≠ H165), L302 (≠ I201), G303 (≠ A202), H306 (≠ M206), E345 (≠ D236), D470 (≠ E340)
- binding manganese (ii) ion: E240 (= E137), D241 (= D138), D264 (= D163)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R150 (≠ A76), N244 (≠ A141), T268 (= T167), A297 (= A196), G298 (= G197), E299 (≠ A198), A300 (= A199), D330 (= D221), S331 (≠ R222), K332 (≠ D223), K346 (= K237), V374 (≠ L262), A375 (≠ S263), A376 (= A264), I377 (vs. gap), L401 (= L285), S402 (≠ A286), N403 (= N287), G447 (≠ V317)
Query Sequence
>WP_024891696.1 NCBI__GCF_000559025.1:WP_024891696.1
MSNDDFKQAALDYHRLSPPGKIKVSATKPMLTQRDLALAYSPGVAYACEEIAADPRAASE
LTARGNLVAVISNGTAVLGLGDIGPLAGKPVMEGKGVLFQKFAGIDVFDIEVDERDPDKL
VEIIASLEPTFGGINLEDIKAPECFIVERKLRERLKIPVFHDDQHGTAIIVGAAVINALE
IAGKRIEDVRLATAGAGAAGIACLDMLVALGLRPENILAVDRDGVLYAGRDNLDPDKARY
ARETDKRSLAEIVEGADIFLGLSAGGVLTPEMVETMAPRPIILALANPYPEILPEHAKRV
RPDCIIATGRSDYPNQVNNALCFPYIFRGALDVGATGINEAMKLACVRAIAALAKEEASD
LGSAYGGETPTFGPEYIIPRPFDQRLLTMLAPAVAQAAMESGVALRPIEDMRAYRDKLGQ
FLYRTGLVMKPVYDRARGDRQRVVYAEGEEEQVLRAVQTVVDERLAHPILIGRPEVIEAR
IRRLGLRLQVGRDFELTNINDDPRFNEYWQQYHAITERRGVTPDSAKNLMRSRPALIAAL
MVQRGEADAMLCGIVGRFHKKLGYIRSVFPLEQGVQSTSAMTGVVNDRGLWFFLDTHVQH
DPTAEQLAESTLQASYRLKLFGIEPKVALLSHSNFGSHEDASASKMRRVREILAQRAPRL
EVDGEMMADTAWDEPLRRRIFPNTTLSGRPNLFVLPNLDAANITYNMVRVMTDGAALGPI
LMGLSAPVHVMTPTATPRRVVNMTAIAAVDAQIRKAQREGQ
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