SitesBLAST
Comparing WP_038203090.1 NCBI__GCF_000745855.1:WP_038203090.1 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: 9:765/766 of query aligns to 2:757/759 of P76558
- K56 (≠ M63) modified: N6-acetyllysine
6zngF Maeb full-length acetyl-coa bound state (see paper)
47% identity, 97% coverage: 19:763/766 of query aligns to 11:744/753 of 6zngF
- active site: Y38 (= Y46), A74 (= A82), K93 (= K101), E135 (= E143), D136 (= D144), D160 (= D168), D161 (= D169), N286 (= N295)
- binding acetyl coenzyme *a: R511 (≠ M526), K514 (≠ R529), Y552 (≠ F568), A553 (≠ D569), R557 (≠ K573), L560 (≠ G576), P571 (= P586), T590 (≠ N607), V591 (= V608), N592 (≠ H609), L593 (≠ E610), Y625 (≠ H642), Q659 (≠ H677), L690 (= L708), N694 (= N712), Q724 (≠ N743)
6zn7A Maeb malic enzyme domain apoprotein (see paper)
60% identity, 52% coverage: 19:415/766 of query aligns to 10:405/405 of 6zn7A
- active site: Y37 (= Y46), A73 (= A82), K92 (= K101), E134 (= E143), D135 (= D144), D159 (= D168), D160 (= D169), N285 (= N295)
- binding magnesium ion: E134 (= E143), D135 (= D144), D160 (= D169)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: T164 (= T173), N191 (≠ S200), A193 (= A202), G194 (= G203), A195 (= A204), S196 (≠ A205), D218 (= D227), S219 (= S228), K235 (= K244), L260 (≠ C270), S261 (= S271), V262 (≠ A272), M283 (≠ L293), N285 (= N295), V315 (= V325)
6zn4A Maeb malic enzyme domain apoprotein (see paper)
60% identity, 52% coverage: 19:415/766 of query aligns to 10:405/406 of 6zn4A
5ceeA Malic enzyme from candidatus phytoplasma aywb in complex with NAD and mg2+ (see paper)
47% identity, 49% coverage: 38:412/766 of query aligns to 26:385/387 of 5ceeA
- active site: Y34 (= Y46), A70 (= A82), K89 (= K101), E131 (= E143), D132 (= D144), D156 (= D168), D157 (= D169), N283 (= N295)
- binding magnesium ion: E131 (= E143), D132 (= D144), D157 (= D169)
- binding nicotinamide-adenine-dinucleotide: T161 (= T173), N188 (≠ S200), G189 (= G201), G191 (= G203), A193 (= A205), D213 (= D227), K214 (≠ S228), V258 (≠ C270), S259 (= S271), I263 (≠ V275), L281 (= L293), N283 (= N295), V312 (= V325), N314 (= N327)
2dvmA NAD complex structure of ph1275 protein from pyrococcus horikoshii
41% identity, 58% coverage: 12:457/766 of query aligns to 1:433/438 of 2dvmA
- active site: Y37 (= Y46), R73 (≠ A82), K92 (= K101), E134 (= E143), D135 (= D144), D159 (= D168), D160 (= D169), N296 (= N295)
- binding nicotinamide-adenine-dinucleotide: T164 (= T173), G194 (= G203), A195 (= A204), A196 (= A205), V217 (≠ C226), E218 (≠ D227), L219 (≠ S228), P224 (≠ Y233), F269 (≠ C270), T270 (≠ S271), L294 (= L293), N296 (= N295), N327 (= N327)
2a9fA Crystal structure of a putative malic enzyme ((s)-malate:nad+ oxidoreductase (decarboxylating))
47% identity, 44% coverage: 26:365/766 of query aligns to 18:354/383 of 2a9fA
2haeD Crystal structure of a putative malic enzyme (malate oxidoreductase)
44% identity, 51% coverage: 16:407/766 of query aligns to 2:373/373 of 2haeD
2haeB Crystal structure of a putative malic enzyme (malate oxidoreductase)
44% identity, 51% coverage: 16:407/766 of query aligns to 2:373/373 of 2haeB
- active site: Y31 (= Y46), A67 (= A82), K86 (= K101), E128 (= E143), D129 (= D144), D153 (= D168), D154 (= D169), N280 (= N295)
- binding nicotinamide-adenine-dinucleotide: T158 (= T173), N185 (≠ S200), G188 (= G203), A189 (= A204), A190 (= A205), D210 (= D227), R211 (≠ S228), V255 (≠ C270), S256 (= S271), R257 (≠ A272), L278 (= L293), A279 (= A294), N280 (= N295), N311 (= N327)
6ioxA Crystal structure of porphyromonas gingivalis phosphotransacetylase in complex with acetyl-coa (see paper)
31% identity, 41% coverage: 449:762/766 of query aligns to 18:334/339 of 6ioxA
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, 42% coverage: 442:766/766 of query aligns to 393:713/714 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)
29% identity, 41% coverage: 451:765/766 of query aligns to 17:331/333 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)
29% identity, 41% coverage: 451:765/766 of query aligns to 16:330/332 of 2af3C
- binding coenzyme a: R86 (≠ M526), S127 (≠ F568), L131 (= L572), V135 (≠ G576), L146 (≠ T590), A147 (≠ L591), G172 (≠ N607), M173 (≠ V608), M173 (≠ V608), V174 (≠ H609), E175 (= E610), N278 (= N712), Y281 (≠ F715), K282 (≠ N716), Q285 (≠ K719), G294 (= G729), P295 (= P730), T297 (≠ L732), D306 (≠ V741), L307 (= L742), S308 (≠ N743)
1xcoD Crystal structure of a phosphotransacetylase from bacillus subtilis in complex with acetylphosphate (see paper)
26% identity, 41% coverage: 452:762/766 of query aligns to 20:324/325 of 1xcoD
1gq2A Malic enzyme from pigeon liver (see paper)
28% identity, 45% coverage: 76:423/766 of query aligns to 137:527/555 of 1gq2A
- active site: R143 (≠ A82), K161 (= K101), E233 (= E143), D234 (= D144), D256 (= D168), D257 (= D169), N396 (= N295)
- binding manganese (ii) ion: K161 (= K101), E233 (= E143), D234 (= D144), D257 (= D169)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R143 (≠ A82), G146 (= G85), N237 (≠ A147), T261 (= T173), G289 (= G201), A290 (= A202), G291 (= G203), E292 (≠ A204), A293 (= A205), V322 (≠ C226), D323 (= D227), S324 (= S228), A368 (≠ S271), I370 (vs. gap), L394 (= L293), N396 (= N295), G440 (≠ V325), N441 (= N326), N442 (= N327)
- binding oxalate ion: R143 (≠ A82), L145 (= L84), D257 (= D169), N396 (= N295), N442 (= N327)
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, 45% coverage: 76:423/766 of query aligns to 138:528/557 of P40927
- D141 (≠ N79) mutation to N: Increases Km for manganese 14-fold. Increases Km for malate 5-fold.
- R144 (≠ A82) binding NADP(+); binding substrate
- K162 (= K101) binding substrate; mutation to A: Decreases kcat 235-fold. no effect on Km for NADP.
- D194 (= D122) mutation to N: No effect on Km for manganese. Increases Km for malate 8-fold.
- E234 (= E143) binding Mn(2+)
- D235 (= D144) binding Mn(2+)
- N238 (≠ A147) binding NADP(+)
- D258 (= D169) binding Mn(2+)
- AGEA 291:294 (≠ AGAA 202:205) binding NADP(+)
- S325 (= S228) binding NADP(+)
- K340 (= K244) mutation to A: Increases Km for NADP 65-fold. No effect on kcat.
- N397 (= N295) binding NADP(+)
- N443 (= N327) binding NADP(+); binding substrate
- D464 (≠ E348) mutation to N: No effect.
P16243 NADP-dependent malic enzyme, chloroplastic; NADP-ME; EC 1.1.1.40 from Zea mays (Maize) (see 3 papers)
28% identity, 46% coverage: 77:426/766 of query aligns to 232:625/636 of P16243
- R237 (≠ A82) mutation to L: Decreases kcat 530-fold. Increases Km for NADP 36-fold and Km for malate 10-fold.
- K255 (= K101) mutation to I: Increases Km for malate 10-fold, and Km for NADP 15-fold. Decreases kcat 200-fold.
- E339 (= E154) mutation to A: No effect on kcat and Km for NADP. Increases Km for malate 2-fold.
- A387 (= A205) mutation to G: Decreases kcat 48-fold. Increases Km for NADP 4-fold. Increases Km for malate 6-fold.
- A392 (≠ L210) 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 244:245) mutation to LL: No effect on kcat and on Km for malate. Increases Km for NADP 9-fold.
- Q503 (≠ L304) mutation to E: No effect on kcat and Km for NADP. Increases Km for malate 2-fold.
- L544 (≠ I334) 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.
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, 52% coverage: 28:429/766 of query aligns to 141:592/623 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, 37% coverage: 76:359/766 of query aligns to 144:481/564 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 (≠ A147), F248 (= F151), I265 (≠ Q170), Q266 (≠ H171), L302 (vs. gap), G303 (vs. gap), H306 (≠ C209), E345 (≠ S243), D470 (≠ E348)
- binding manganese (ii) ion: E240 (= E143), D241 (= D144), D264 (= D169)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R150 (≠ A82), N244 (≠ A147), T268 (= T173), A297 (= A202), G298 (= G203), E299 (≠ A204), A300 (= A205), D330 (= D227), S331 (= S228), K332 (= K229), K346 (= K244), V374 (≠ C270), A375 (≠ S271), A376 (= A272), I377 (vs. gap), L401 (= L293), S402 (≠ A294), N403 (= N295), G447 (≠ V325)
6w29A Trypanosoma cruzi malic enzyme in complex with inhibitor (mec013) (see paper)
28% identity, 39% coverage: 74:368/766 of query aligns to 133:488/545 of 6w29A
Sites not aligning to the query:
Query Sequence
>WP_038203090.1 NCBI__GCF_000745855.1:WP_038203090.1
MTQKLSPAEEALRDAAREYHRAGVRGKISVTPTKALVNQRDLSLAYSPGVAYPCLDIQAD
PAMAAEFTARGNLVGVVTNGTAVLGLGDIGPLAGKPVMEGKGCLFKKFAGIDVFDIELAE
RDPDKLVDIIASLEPTLGGINLEDIKAPECFYIEKKLRERMNIPVFHDDQHGTAIISAAA
LLNGLELVGKKIGDVKIAVSGAGAAAIACLDVMVGLGAKPANIHACDSKGLIYMGRAGGF
DDSKARYAQKDTGARTLADVVKGADVFLGCSAPGVLTPEMVGTMADKPIILALANPEPEI
RPELAKQVRPDCIIATGRSDYANQVNNVLCFPYIFRGALDCGASKITEEMKLACVREIAD
LTKADISEEVATAYAGQELAFGPDYIIPKPFDSRLILRIAPAVAKAAADSGVATRPIEDL
DAYRQHLSRFVYQTGMFMRPVFTAAKLAQKKRVAYAEGEDERVLRAAQMAVDEGLARPIL
IGRPDIIAMRIQKAGLHLRVGEDAEVVDPENDPRFRQYWEAYHELMGRRGINPEGSKAMV
RRSNTTIAALMVHLGDADAMICGLVGRFDSHLKILGQLLGTQQGVPDFATLNALMLDKYT
LFIADTNVHEDPTAEQLANIALMAAEEVRRFGLPPKVAFLSHSNFGTSERASARKMRVAR
DLFAQMAPDIECDGEMHGDAALSETVRRQALPGSTLTGEANLLICPNLDAANILFNVLKM
TGANGVTVGPILLGSSKPAHVLNPSATVRRVLNMTALAVADANIQR
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