SitesBLAST
Comparing WP_004323552.1 NCBI__GCF_000310185.1:WP_004323552.1 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)
66% identity, 99% coverage: 1:757/764 of query aligns to 1:755/759 of P76558
- K56 (≠ E56) modified: N6-acetyllysine
6zngF Maeb full-length acetyl-coa bound state (see paper)
47% identity, 99% coverage: 4:757/764 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 (= N287)
- binding acetyl coenzyme *a: R511 (≠ M520), K514 (≠ D523), Y552 (= Y562), A553 (≠ D563), R557 (≠ K567), L560 (≠ A570), P571 (≠ Q581), T590 (≠ Y601), V591 (= V602), N592 (= N603), L593 (≠ E604), Y625 (≠ H636), Q659 (≠ H671), L690 (= L702), N694 (= N706), Q724 (≠ T737)
6zn7A Maeb malic enzyme domain apoprotein (see paper)
59% identity, 53% coverage: 4:407/764 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 (= N287)
- 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 (= K237), L260 (= L262), S261 (= S263), V262 (≠ T264), M283 (≠ L285), N285 (= N287), V315 (= V317)
6zn4A Maeb malic enzyme domain apoprotein (see paper)
59% identity, 53% coverage: 4:407/764 of query aligns to 2:405/406 of 6zn4A
2dvmA NAD complex structure of ph1275 protein from pyrococcus horikoshii
46% identity, 52% coverage: 9:405/764 of query aligns to 5:397/438 of 2dvmA
- active site: Y37 (= Y39), R73 (≠ A75), K92 (= K94), E134 (= E136), D135 (= D137), D159 (= D161), D160 (= D162), N296 (= N287)
- binding nicotinamide-adenine-dinucleotide: T164 (= T166), G194 (= G196), A195 (= A197), A196 (= A198), V217 (≠ C219), E218 (≠ D220), L219 (≠ I225), P224 (≠ E230), F269 (≠ L262), T270 (≠ S263), L294 (= L285), N296 (= N287), N327 (= N319)
5ceeA Malic enzyme from candidatus phytoplasma aywb in complex with NAD and mg2+ (see paper)
46% identity, 49% coverage: 31:404/764 of query aligns to 26:385/387 of 5ceeA
- active site: Y34 (= Y39), A70 (= A75), K89 (= K94), E131 (= E136), D132 (= D137), D156 (= D161), D157 (= D162), N283 (= N287)
- 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 (≠ L262), S259 (= S263), I263 (≠ V267), L281 (= L285), N283 (= N287), V312 (= V317), N314 (= N319)
2a9fA Crystal structure of a putative malic enzyme ((s)-malate:nad+ oxidoreductase (decarboxylating))
47% identity, 46% coverage: 19:366/764 of query aligns to 18:366/383 of 2a9fA
2haeD Crystal structure of a putative malic enzyme (malate oxidoreductase)
46% identity, 47% coverage: 9:366/764 of query aligns to 2:357/373 of 2haeD
2haeB Crystal structure of a putative malic enzyme (malate oxidoreductase)
46% identity, 47% coverage: 9:366/764 of query aligns to 2:357/373 of 2haeB
- active site: Y31 (= Y39), A67 (= A75), K86 (= K94), E128 (= E136), D129 (= D137), D153 (= D161), D154 (= D162), N280 (= N287)
- binding nicotinamide-adenine-dinucleotide: T158 (= T166), N185 (≠ S193), G188 (= G196), A189 (= A197), A190 (= A198), D210 (= D220), R211 (≠ S221), V255 (≠ L262), S256 (= S263), R257 (≠ T264), L278 (= L285), A279 (= A286), N280 (= N287), N311 (= N319)
Q8ZND6 Phosphate acetyltransferase; Phosphotransacetylase; EC 2.3.1.222; EC 2.3.1.8 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
30% identity, 41% coverage: 445:761/764 of query aligns to 404:714/714 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)
32% identity, 41% coverage: 444:758/764 of query aligns to 19:339/339 of 6ioxA
1xcoD Crystal structure of a phosphotransacetylase from bacillus subtilis in complex with acetylphosphate (see paper)
29% identity, 41% coverage: 446:756/764 of query aligns to 20:324/325 of 1xcoD
2af3C Phosphotransacetylase from methanosarcina thermophila soaked with coenzyme a (see paper)
28% identity, 41% coverage: 445:756/764 of query aligns to 16:327/332 of 2af3C
- binding coenzyme a: R86 (≠ M520), S127 (≠ Y562), L131 (= L566), V135 (≠ A570), L146 (≠ Q581), A147 (≠ F582), G172 (≠ Y601), M173 (≠ V602), M173 (≠ V602), V174 (≠ N603), E175 (= E604), N278 (= N706), Y281 (≠ F709), K282 (≠ N710), Q285 (≠ M712), G294 (= G723), P295 (= P724), T297 (≠ L726), D306 (≠ I735), L307 (≠ V736), S308 (≠ T737)
P38503 Phosphate acetyltransferase; Phosphotransacetylase; EC 2.3.1.8 from Methanosarcina thermophila (see 2 papers)
28% identity, 41% coverage: 445:756/764 of query aligns to 17:328/333 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)
26% identity, 50% coverage: 35:418/764 of query aligns to 180:625/636 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 (≠ KA 237:238) mutation to LL: No effect on kcat and on Km for malate. Increases Km for NADP 9-fold.
- Q503 (≠ K298) 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.
1gq2A Malic enzyme from pigeon liver (see paper)
26% identity, 52% coverage: 32:426/764 of query aligns to 83:544/555 of 1gq2A
- active site: Y90 (= Y39), R143 (≠ A75), K161 (vs. gap), E233 (= E136), D234 (= D137), D256 (= D161), D257 (= D162), N396 (= N287)
- binding manganese (ii) ion: K161 (vs. gap), 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 (≠ C219), D323 (= D220), S324 (= S221), A368 (≠ S263), I370 (vs. gap), L394 (= L285), N396 (= N287), G440 (≠ V317), N441 (= N318), N442 (= N319)
- binding oxalate ion: R143 (≠ A75), L145 (= L77), D257 (= D162), 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, 52% coverage: 32:426/764 of query aligns to 84:545/557 of P40927
- D141 (≠ N72) mutation to N: Increases Km for manganese 14-fold. Increases Km for malate 5-fold.
- R144 (≠ A75) binding NADP(+); binding substrate
- K162 (vs. gap) binding substrate; mutation to A: Decreases kcat 235-fold. no effect on Km for NADP.
- D194 (≠ K100) mutation to N: No effect on Km for manganese. Increases Km for malate 8-fold.
- E234 (= E136) binding Mn(2+)
- D235 (= D137) binding Mn(2+)
- N238 (≠ A140) binding NADP(+)
- D258 (= D162) binding Mn(2+)
- AGEA 291:294 (≠ AGAA 195:198) binding NADP(+)
- S325 (= S221) 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.
6c7nB Monoclinic form of malic enzyme from sorghum at 2 angstroms resolution (see paper)
26% identity, 40% coverage: 35:342/764 of query aligns to 97:477/553 of 6c7nB
- active site: Y101 (= Y39), R154 (≠ A75), K172 (vs. gap), E244 (= E136), D245 (= D137), D267 (= D161), D268 (= D162), L348 (≠ M233), N409 (= N287)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R154 (≠ A75), L156 (= L77), G157 (= G78), N248 (≠ A140), T272 (= T166), L299 (≠ S193), G300 (= G194), A301 (= A195), G302 (= G196), E303 (≠ A197), A304 (= A198), D335 (= D220), S336 (= S221), K352 (= K237), T380 (= T264), S381 (≠ A265), L407 (= L285), S408 (≠ A286), N409 (= N287), S452 (≠ V317), N454 (= N319)
- binding pyruvic acid: Y101 (= Y39), R154 (≠ A75), L156 (= L77)
Sites not aligning to the query:
6c7nA Monoclinic form of malic enzyme from sorghum at 2 angstroms resolution (see paper)
26% identity, 40% coverage: 35:342/764 of query aligns to 97:477/553 of 6c7nA
- active site: Y101 (= Y39), R154 (≠ A75), K172 (vs. gap), E244 (= E136), D245 (= D137), D267 (= D161), D268 (= D162), L348 (≠ M233), N409 (= N287)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: T272 (= T166), L299 (≠ S193), G300 (= G194), A301 (= A195), G302 (= G196), E303 (≠ A197), A304 (= A198), D335 (= D220), S336 (= S221), K352 (= K237), T380 (= T264), S381 (≠ A265), L407 (= L285), S408 (≠ A286), N409 (= N287), S452 (≠ V317)
Sites not aligning to the query:
6w49A Trypanosoma cruzi malic enzyme in complex with inhibitor (mec010) (see paper)
24% identity, 41% coverage: 35:350/764 of query aligns to 82:475/543 of 6w49A
Query Sequence
>WP_004323552.1 NCBI__GCF_000310185.1:WP_004323552.1
MDQDFITAALDYHRSPTRGKISVVPTKGLTNQRDLALAYSPGVAAACDAIVADPAEAFEL
TSRGNLVAVVTNGTAVLGLGNIGPLASKPVMEGKGCLFKKFANIDVFDIELAENDPDKLI
EIIAALEPTLGGINLEDIKAPECFYIEKKLRERMKIPVFHDDQHGTAIISAAGLVNGLKV
VGKNIADVKLVCSGAGAAAIACLDMMVSVGLRRENIYVCDSKGVIYEGREPNMEPTKARY
AQKTEGRALGDVIAGADVFLGLSTAGVLKPEMVAKMAAKPLIFALANPNPEILPADAKAV
RPDCIVATGRSDFPNQVNNVLCFPFIFRGALDVGATTINEEMKLACVKAIAELAEAEASD
IVASAYGGQELSFGSEYIIPKPFDPRLIVKIAPAVAKAAMDSGVATKPIADLEAYASSLN
AFVYQSGIVMKPVFSAAKAVPLEQKRVIYAEGEDERVLHAVRVVLDEGLARPILIGRPEV
IEMRIKKIGLNLKPERDFEIVNPESDPRYRELWTEYYKLMKRDGVTPDLAKAKIRRDTTL
IGVMMLRRGDADALVCGTFGSYDYHLKQVADVIGLAPGAKQFAAMNLLLLTKRMLAITDT
YVNENPSAEEVAEIARMASDELRRFGIEPSVALLSHSNFGSSNSASARKMRRACEILRET
SPDLNVDGEMHGDAALSEEIRDKLHPDSGLKGEANLLVMPNLDAANISFNLMKVANGDGV
SVGPILLGAAKPVHIVTPSATVRRLVNMTALAVVDAKESRNAGA
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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