SitesBLAST
Comparing CA265_RS19000 FitnessBrowser__Pedo557:CA265_RS19000 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)
6zngF Maeb full-length acetyl-coa bound state (see paper)
51% identity, 98% coverage: 4:760/771 of query aligns to 2:753/753 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 (= R515), K514 (= K518), Y552 (= Y556), A553 (≠ G557), R557 (≠ K561), L560 (= L564), P571 (≠ V576), T590 (= T595), V591 (= V596), N592 (= N597), L593 (≠ V598), Y625 (= Y630), Q659 (= Q665), L690 (= L697), N694 (= N701), Q724 (= Q731)
P76558 NADP-dependent malic enzyme; NADP-ME; EC 1.1.1.40 from Escherichia coli (strain K12) (see paper)
50% identity, 97% coverage: 7:753/771 of query aligns to 6:757/759 of P76558
- K56 (≠ D57) modified: N6-acetyllysine
6zn4A Maeb malic enzyme domain apoprotein (see paper)
63% identity, 52% coverage: 4:407/771 of query aligns to 1:405/406 of 6zn4A
6zn7A Maeb malic enzyme domain apoprotein (see paper)
63% identity, 52% coverage: 4:407/771 of query aligns to 1:405/405 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 (= N194), A193 (= A196), G194 (= G197), A195 (= A198), S196 (≠ A199), D218 (= D221), S219 (≠ R222), K235 (= K237), L260 (= L262), S261 (= S263), V262 (≠ S264), M283 (= M285), N285 (= N287), V315 (= V317)
5ceeA Malic enzyme from candidatus phytoplasma aywb in complex with NAD and mg2+ (see paper)
47% identity, 48% coverage: 35:406/771 of query aligns to 29:387/387 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 (= N194), G189 (= G195), G191 (= G197), A193 (= A199), D213 (= D221), K214 (≠ R222), V258 (≠ L262), S259 (= S263), I263 (≠ C267), L281 (≠ M285), N283 (= N287), V312 (= V317), N314 (= N319)
2a9fA Crystal structure of a putative malic enzyme ((s)-malate:nad+ oxidoreductase (decarboxylating))
48% identity, 47% coverage: 20:383/771 of query aligns to 18:378/383 of 2a9fA
2dvmA NAD complex structure of ph1275 protein from pyrococcus horikoshii
44% identity, 53% coverage: 7:412/771 of query aligns to 2:405/438 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 (≠ C220), E218 (≠ D221), L219 (≠ R222), P224 (≠ D229), F269 (≠ L262), T270 (≠ S263), L294 (≠ M285), N296 (= N287), N327 (= N319)
2haeD Crystal structure of a putative malic enzyme (malate oxidoreductase)
43% identity, 51% coverage: 9:399/771 of query aligns to 1:373/373 of 2haeD
2haeB Crystal structure of a putative malic enzyme (malate oxidoreductase)
43% identity, 51% coverage: 9:399/771 of query aligns to 1:373/373 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 (= N194), G188 (= G197), A189 (= A198), A190 (= A199), D210 (= D221), R211 (= R222), V255 (≠ L262), S256 (= S263), R257 (≠ S264), L278 (≠ M285), A279 (= A286), N280 (= N287), N311 (= N319)
6ioxA Crystal structure of porphyromonas gingivalis phosphotransacetylase in complex with acetyl-coa (see paper)
37% identity, 42% coverage: 423:745/771 of query aligns to 3:329/339 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)
33% identity, 46% coverage: 400:755/771 of query aligns to 360:712/714 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.
1xcoD Crystal structure of a phosphotransacetylase from bacillus subtilis in complex with acetylphosphate (see paper)
35% identity, 39% coverage: 443:745/771 of query aligns to 20:319/325 of 1xcoD
2af3C Phosphotransacetylase from methanosarcina thermophila soaked with coenzyme a (see paper)
29% identity, 42% coverage: 429:755/771 of query aligns to 3:332/332 of 2af3C
- binding coenzyme a: R86 (= R515), S127 (≠ Y556), L131 (≠ I560), V135 (≠ L564), L146 (≠ R575), A147 (≠ V576), G172 (≠ T595), M173 (≠ V596), M173 (≠ V596), V174 (≠ N597), E175 (≠ V598), N278 (= N701), Y281 (= Y704), K282 (= K705), Q285 (= Q708), G294 (= G717), P295 (= P718), T297 (≠ L720), D306 (≠ I729), L307 (≠ V730), S308 (≠ Q731)
P38503 Phosphate acetyltransferase; Phosphotransacetylase; EC 2.3.1.8 from Methanosarcina thermophila (see 2 papers)
29% identity, 42% coverage: 429:755/771 of query aligns to 4:333/333 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
P40927 NADP-dependent malic enzyme; NADP-ME; EC 1.1.1.40 from Columba livia (Rock dove) (see 3 papers)
26% identity, 44% coverage: 70:405/771 of query aligns to 138:516/557 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 (vs. gap) binding substrate; mutation to A: Decreases kcat 235-fold. no effect on Km for NADP.
- D194 (≠ I101) 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 (≠ E352) mutation to N: No effect.
1gq2A Malic enzyme from pigeon liver (see paper)
26% identity, 44% coverage: 70:405/771 of query aligns to 137:515/555 of 1gq2A
- active site: R143 (≠ A76), K161 (vs. gap), E233 (= E137), D234 (= D138), D256 (= D162), D257 (= D163), N396 (= N287)
- binding manganese (ii) ion: K161 (vs. gap), 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 (≠ C220), D323 (= D221), S324 (≠ R222), A368 (≠ S263), I370 (vs. gap), L394 (≠ M285), N396 (= N287), G440 (≠ V317), N441 (= N318), N442 (= N319)
- binding oxalate ion: R143 (≠ A76), L145 (= L78), D257 (= D163), N396 (= N287), N442 (= N319)
Sites not aligning to the query:
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)
25% identity, 45% coverage: 58:401/771 of query aligns to 178:579/623 of Q9SIU0
Sites not aligning to the query:
- 122 R→A: Impaired fumarate-mediated allosteric activation.
8eyoA Crystal structure of human mitochondrial NADP+ malic enzyme 3 with NADP bound (see paper)
27% identity, 35% coverage: 70:340/771 of query aligns to 136:459/562 of 8eyoA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: T260 (= T167), Q287 (≠ N194), A289 (= A196), G290 (= G197), E291 (≠ A198), A292 (= A199), D322 (= D221), S323 (≠ R222), K338 (= K237), V366 (≠ L262), A367 (≠ S263), I369 (vs. gap), L393 (≠ M285), S394 (≠ A286), N395 (= N287), G439 (≠ V317), N441 (= N319)
7x11A Crystal structure of me1 in complex with NADPH (see paper)
26% identity, 35% coverage: 70:340/771 of query aligns to 144:467/564 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 (≠ S202), H306 (≠ K205), E345 (≠ I236)
- 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 (≠ S223), K346 (= K237), V374 (≠ L262), A375 (≠ S263), A376 (≠ S264), I377 (vs. gap), L401 (≠ M285), S402 (≠ A286), N403 (= N287), G447 (≠ V317)
Sites not aligning to the query:
6w49A Trypanosoma cruzi malic enzyme in complex with inhibitor (mec010) (see paper)
24% identity, 44% coverage: 36:377/771 of query aligns to 82:490/543 of 6w49A
Query Sequence
>CA265_RS19000 FitnessBrowser__Pedo557:CA265_RS19000
MSKTTRKQDALDYHSQGRPGKIQVVPTKPTTSQRDLTLAYSPGVAEPCLKIAENKEDVYK
YTAKGNLVAVISNGTAVLGLGDIGPEAGKPVMEGKGLLFKIFADIDVFDLELDTKNVDDF
VKIVKALEPTFGGVNLEDIKAPECFEIERRLKEEMNIPVMHDDQHGTAIISAAALLNACE
IFKKKMDKIKIVVNGAGAAAISCTKLYVSLGAKKENIIMCDRSGVIRKDREVLDEIKAEF
ATDRKISTLAEAMKDSDVFIGLSSADCVTAEMLTSMAKNPIVFAMANPNPEIAYELAIKT
RKDIIMATGRSDYPNQVNNVLGFPYIFRGALDVRATGINEPMKIAAVKAIAELAKKSVPE
AVNLAYNARNLKFGKEYIIPKPVDFRLITEVSIAVAKAAIESGVARKIITDWDAYSEELR
KRLGLDDAIMRAITTKAKTDPKRVVFAEADNYKILKAAQIVNDENIAIPILLGNKDKIQA
IIDEHGLELEGVEIIDQMQNPDKTKQYAEALYQKRQRKGVSLTDATKLLRDRNYYGASMV
EFGEADAMISGLTKNYGSTIKPALHVIGVDPSVKRVAGMYMMMTKKGPVFFGDTTVNVDP
TAEELVDITLLLDKSVKQFNIKPRIALLSYSNFGSNDGVTPNKVRETVKLLHKNHPEVIV
DGEMQGNFAINNELLKDNFPFSTLADAPANTLVFPNLESGNIAYKLLQELGGAEAVGPIL
LGLNKPVHIVQLGSSVREIVNMVTIAVVDVQAKEEIATSKRKGIFGKTTKK
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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