SitesBLAST
Comparing 3610086 FitnessBrowser__Dino:3610086 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)
6zngF Maeb full-length acetyl-coa bound state (see paper)
47% identity, 98% coverage: 10:748/752 of query aligns to 6:740/753 of 6zngF
- active site: Y38 (= Y42), A74 (= A78), K93 (= K97), E135 (= E139), D136 (= D140), D160 (= D164), D161 (= D165), N286 (= N290)
- binding acetyl coenzyme *a: R511 (≠ L518), K514 (= K521), Y552 (≠ S560), A553 (= A561), R557 (≠ G565), L560 (≠ N568), P571 (≠ A579), T590 (≠ L598), V591 (= V599), N592 (≠ H600), L593 (≠ E601), Y625 (≠ F633), Q659 (≠ T668), L690 (≠ R698), N694 (≠ S702), Q724 (≠ S732)
P76558 NADP-dependent malic enzyme; NADP-ME; EC 1.1.1.40 from Escherichia coli (strain K12) (see paper)
46% identity, 98% coverage: 9:747/752 of query aligns to 6:750/759 of P76558
- K56 (≠ T59) modified: N6-acetyllysine
6zn4A Maeb malic enzyme domain apoprotein (see paper)
61% identity, 53% coverage: 10:409/752 of query aligns to 5:405/406 of 6zn4A
6zn7A Maeb malic enzyme domain apoprotein (see paper)
61% identity, 53% coverage: 10:409/752 of query aligns to 5:405/405 of 6zn7A
- active site: Y37 (= Y42), A73 (= A78), K92 (= K97), E134 (= E139), D135 (= D140), D159 (= D164), D160 (= D165), N285 (= N290)
- binding magnesium ion: E134 (= E139), D135 (= D140), D160 (= D165)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: T164 (= T169), N191 (= N196), A193 (= A198), G194 (= G199), A195 (= A200), S196 (≠ A201), D218 (= D223), S219 (≠ T224), K235 (= K240), L260 (≠ V265), S261 (= S266), V262 (= V267), M283 (= M288), N285 (= N290), V315 (= V320)
5ceeA Malic enzyme from candidatus phytoplasma aywb in complex with NAD and mg2+ (see paper)
46% identity, 53% coverage: 9:408/752 of query aligns to 2:387/387 of 5ceeA
- active site: Y34 (= Y42), A70 (= A78), K89 (= K97), E131 (= E139), D132 (= D140), D156 (= D164), D157 (= D165), N283 (= N290)
- binding magnesium ion: E131 (= E139), D132 (= D140), D157 (= D165)
- binding nicotinamide-adenine-dinucleotide: T161 (= T169), N188 (= N196), G189 (= G197), G191 (= G199), A193 (= A201), D213 (= D223), K214 (≠ T224), V258 (= V265), S259 (= S266), I263 (≠ A270), L281 (≠ M288), N283 (= N290), V312 (= V320), N314 (= N322)
2dvmA NAD complex structure of ph1275 protein from pyrococcus horikoshii
44% identity, 55% coverage: 9:422/752 of query aligns to 2:412/438 of 2dvmA
- active site: Y37 (= Y42), R73 (≠ A78), K92 (= K97), E134 (= E139), D135 (= D140), D159 (= D164), D160 (= D165), N296 (= N290)
- binding nicotinamide-adenine-dinucleotide: T164 (= T169), G194 (= G199), A195 (= A200), A196 (= A201), V217 (≠ C222), E218 (≠ D223), L219 (≠ I228), P224 (≠ T233), F269 (≠ V265), T270 (≠ S266), L294 (≠ M288), N296 (= N290), N327 (= N322)
2a9fA Crystal structure of a putative malic enzyme ((s)-malate:nad+ oxidoreductase (decarboxylating))
51% identity, 45% coverage: 22:360/752 of query aligns to 18:354/383 of 2a9fA
2haeD Crystal structure of a putative malic enzyme (malate oxidoreductase)
47% identity, 44% coverage: 22:354/752 of query aligns to 11:342/373 of 2haeD
2haeB Crystal structure of a putative malic enzyme (malate oxidoreductase)
47% identity, 44% coverage: 22:354/752 of query aligns to 11:342/373 of 2haeB
- active site: Y31 (= Y42), A67 (= A78), K86 (= K97), E128 (= E139), D129 (= D140), D153 (= D164), D154 (= D165), N280 (= N290)
- binding nicotinamide-adenine-dinucleotide: T158 (= T169), N185 (= N196), G188 (= G199), A189 (= A200), A190 (= A201), D210 (= D223), R211 (≠ T224), V255 (= V265), S256 (= S266), R257 (≠ V267), L278 (≠ M288), A279 (= A289), N280 (= N290), N311 (= N322)
1xcoD Crystal structure of a phosphotransacetylase from bacillus subtilis in complex with acetylphosphate (see paper)
28% identity, 43% coverage: 429:750/752 of query aligns to 4:323/325 of 1xcoD
6ioxA Crystal structure of porphyromonas gingivalis phosphotransacetylase in complex with acetyl-coa (see paper)
29% identity, 43% coverage: 429:748/752 of query aligns to 5:331/339 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)
27% identity, 43% coverage: 424:750/752 of query aligns to 385:708/714 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)
28% identity, 43% coverage: 430:749/752 of query aligns to 3:325/333 of P38503
- C159 (≠ G578) 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)
28% identity, 43% coverage: 430:749/752 of query aligns to 2:324/332 of 2af3C
- binding coenzyme a: R86 (≠ L518), S127 (= S560), L131 (= L564), V135 (vs. gap), L146 (= L566), A147 (≠ I567), G172 (≠ L598), M173 (≠ V599), M173 (≠ V599), V174 (≠ H600), E175 (= E601), N278 (≠ S702), Y281 (≠ V705), K282 (= K706), Q285 (= Q709), G294 (= G718), P295 (= P719), T297 (≠ L721), D306 (≠ L730), L307 (≠ C731), S308 (= S732)
P16243 NADP-dependent malic enzyme, chloroplastic; NADP-ME; EC 1.1.1.40 from Zea mays (Maize) (see 3 papers)
26% identity, 51% coverage: 38:420/752 of query aligns to 180:625/636 of P16243
- R237 (≠ A78) mutation to L: Decreases kcat 530-fold. Increases Km for NADP 36-fold and Km for malate 10-fold.
- K255 (= K97) mutation to I: Increases Km for malate 10-fold, and Km for NADP 15-fold. Decreases kcat 200-fold.
- E339 (= E150) mutation to A: No effect on kcat and Km for NADP. Increases Km for malate 2-fold.
- A387 (= A201) mutation to G: Decreases kcat 48-fold. Increases Km for NADP 4-fold. Increases Km for malate 6-fold.
- A392 (≠ I206) mutation to G: No effect on kcat. Increases Km for NADP 3.5-fold. Increases Km for malate 2.5-fold.
- KK 435:436 (≠ KS 240:241) mutation to LL: No effect on kcat and on Km for malate. Increases Km for NADP 9-fold.
- Q503 (≠ E299) mutation to E: No effect on kcat and Km for NADP. Increases Km for malate 2-fold.
- L544 (= L329) 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.
P40927 NADP-dependent malic enzyme; NADP-ME; EC 1.1.1.40 from Columba livia (Rock dove) (see 3 papers)
27% identity, 38% coverage: 72:360/752 of query aligns to 138:481/557 of P40927
- D141 (≠ N75) mutation to N: Increases Km for manganese 14-fold. Increases Km for malate 5-fold.
- R144 (≠ A78) binding ; binding
- K162 (= K97) binding ; mutation to A: Decreases kcat 235-fold. no effect on Km for NADP.
- D194 (= D118) mutation to N: No effect on Km for manganese. Increases Km for malate 8-fold.
- E234 (= E139) binding
- D235 (= D140) binding
- N238 (≠ A143) binding
- D258 (= D165) binding
- AGEA 291:294 (≠ AGAA 198:201) binding
- S325 (≠ T224) binding
- K340 (≠ W239) mutation to A: Increases Km for NADP 65-fold. No effect on kcat.
- N397 (= N290) binding
- N443 (= N322) binding ; binding
- D464 (= D343) mutation to N: No effect.
1gq2A Malic enzyme from pigeon liver (see paper)
27% identity, 38% coverage: 72:360/752 of query aligns to 137:480/555 of 1gq2A
- active site: R143 (≠ A78), K161 (= K97), E233 (= E139), D234 (= D140), D256 (= D164), D257 (= D165), N396 (= N290)
- binding manganese (ii) ion: K161 (= K97), E233 (= E139), D234 (= D140), D257 (= D165)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R143 (≠ A78), G146 (= G81), N237 (≠ A143), T261 (= T169), G289 (= G197), A290 (= A198), G291 (= G199), E292 (≠ A200), A293 (= A201), V322 (≠ C222), D323 (= D223), S324 (≠ T224), A368 (vs. gap), I370 (≠ V267), L394 (≠ M288), N396 (= N290), G440 (≠ V320), N441 (= N321), N442 (= N322)
- binding oxalate ion: R143 (≠ A78), L145 (= L80), D257 (= D165), N396 (= N290), N442 (= N322)
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)
28% identity, 42% coverage: 45:360/752 of query aligns to 163:548/623 of Q9SIU0
Sites not aligning to the query:
- 122 R→A: Impaired fumarate-mediated allosteric activation.
6c7nB Monoclinic form of malic enzyme from sorghum at 2 angstroms resolution (see paper)
27% identity, 43% coverage: 38:360/752 of query aligns to 97:492/553 of 6c7nB
- active site: Y101 (= Y42), R154 (≠ A78), K172 (= K97), E244 (= E139), D245 (= D140), D267 (= D164), D268 (= D165), L348 (≠ M236), N409 (= N290)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R154 (≠ A78), L156 (= L80), G157 (= G81), N248 (≠ A143), T272 (= T169), L299 (≠ N196), G300 (= G197), A301 (= A198), G302 (= G199), E303 (≠ A200), A304 (= A201), D335 (= D223), S336 (≠ T224), K352 (= K240), T380 (≠ V265), S381 (= S266), L407 (≠ M288), S408 (≠ A289), N409 (= N290), S452 (≠ V320), N454 (= N322)
- binding pyruvic acid: Y101 (= Y42), R154 (≠ A78), L156 (= L80)
Sites not aligning to the query:
6c7nA Monoclinic form of malic enzyme from sorghum at 2 angstroms resolution (see paper)
27% identity, 43% coverage: 38:360/752 of query aligns to 97:492/553 of 6c7nA
- active site: Y101 (= Y42), R154 (≠ A78), K172 (= K97), E244 (= E139), D245 (= D140), D267 (= D164), D268 (= D165), L348 (≠ M236), N409 (= N290)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: T272 (= T169), L299 (≠ N196), G300 (= G197), A301 (= A198), G302 (= G199), E303 (≠ A200), A304 (= A201), D335 (= D223), S336 (≠ T224), K352 (= K240), T380 (≠ V265), S381 (= S266), L407 (≠ M288), S408 (≠ A289), N409 (= N290), S452 (≠ V320)
Sites not aligning to the query:
Query Sequence
>3610086 FitnessBrowser__Dino:3610086
MSGNNKITREEALAYHLEPTPGKLEVSASTPMSTQRDLSLAYSPGVAVPCEAIAENPETA
YDYTTKGNLVAVITNGSAVLGLGNLGALASKPVMEGKSVLFKRFADVNSIDIELDTEDPD
AIIQAVKLMAPTFGGVNLEDIKAPECFIIEQTLKEQLDIPVFHDDQHGTAVITAAGLLNA
LRLTGKAIEDCKIVLNGAGAAGIACIELIKAMGAKPQNCIVCDTKGVIFQGRTEGMNQWK
SAHAVKTEMRTLDDAMKGADVFLGVSVKGAVTQAMLESMADDPVIFAMANPDPEITPEEA
HAIRPDAIVATGRSDYPNQVNNVLGFPYLFRGALDIRARAINDEMKIACAEALADLARED
VPDEVALAYGRKLSFGRDYIIPTPFDPRLIHTVPLAVAKAGMDTGVARRPIVDMDGYEQS
LRARMDPTASMLQGMFARAKGTQARMIFAEGDDIRVLRAAVTYQRSGLGKALVVGRQDDV
KTRLEAAGIGDAFRELEIVNAGNTRHLETYKEFLYGRLQRKGYDTSDIHRLAARDRHAFS
ALMLAHGHGDGLVTGATRKSAHVLGLINTVFDAGAEDGAVGVTALLVKGRIVLIADTLVH
EWPDEEDLADIATRAAGTARSLGLEPRVAFVSFSTFGYPVSERATKMHRAPRVLDARGVD
FEYDGEMTVDVALDPEIMAQYPFCRLSGPANVLVVPARHSASISVKLMQQLGDATVIGPI
LSGVGKPIQLCSATSTANDILNMAVLAACRVG
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