SitesBLAST
Comparing 16562 FitnessBrowser__Keio:16562 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)
100% identity, 100% coverage: 1:759/759 of query aligns to 1:759/759 of P76558
- K56 (= K56) modified: N6-acetyllysine
6zngF Maeb full-length acetyl-coa bound state (see paper)
49% identity, 99% coverage: 4:755/759 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 (= N288)
- binding acetyl coenzyme *a: R511 (≠ M518), K514 (≠ R521), Y552 (= Y560), A553 (≠ H561), R557 (≠ S565), L560 (≠ K568), P571 (≠ A580), T590 (≠ Y599), V591 (= V600), N592 (= N601), L593 (≠ D602), Y625 (≠ H634), Q659 (≠ H669), L690 (≠ M700), N694 (≠ R704), Q724 (≠ T735)
6zn4A Maeb malic enzyme domain apoprotein (see paper)
62% identity, 53% coverage: 4:408/759 of query aligns to 2:405/406 of 6zn4A
6zn7A Maeb malic enzyme domain apoprotein (see paper)
62% identity, 53% coverage: 4:408/759 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 (= N288)
- 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 (≠ C263), S261 (= S264), V262 (≠ G265), M283 (≠ L286), N285 (= N288), V315 (= V318)
5ceeA Malic enzyme from candidatus phytoplasma aywb in complex with NAD and mg2+ (see paper)
48% identity, 49% coverage: 34:405/759 of query aligns to 29:385/387 of 5ceeA
- active site: Y34 (= Y39), A70 (= A75), K89 (= K94), E131 (= E136), D132 (= D137), D156 (= D161), D157 (= D162), N283 (= N288)
- 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 (≠ C263), S259 (= S264), I263 (≠ V268), L281 (= L286), N283 (= N288), V312 (= V318), N314 (= N320)
2dvmA NAD complex structure of ph1275 protein from pyrococcus horikoshii
46% identity, 53% coverage: 5:406/759 of query aligns to 1:397/438 of 2dvmA
- active site: Y37 (= Y39), R73 (≠ A75), K92 (= K94), E134 (= E136), D135 (= D137), D159 (= D161), D160 (= D162), N296 (= N288)
- binding nicotinamide-adenine-dinucleotide: T164 (= T166), G194 (= G196), A195 (= A197), A196 (= A198), V217 (≠ C219), E218 (≠ D220), L219 (≠ I225), P224 (= P231), F269 (≠ C263), T270 (≠ S264), L294 (= L286), N296 (= N288), N327 (= N320)
2a9fA Crystal structure of a putative malic enzyme ((s)-malate:nad+ oxidoreductase (decarboxylating))
50% identity, 47% coverage: 1:354/759 of query aligns to 1:350/383 of 2a9fA
2haeD Crystal structure of a putative malic enzyme (malate oxidoreductase)
45% identity, 52% coverage: 9:400/759 of query aligns to 2:373/373 of 2haeD
2haeB Crystal structure of a putative malic enzyme (malate oxidoreductase)
45% identity, 52% coverage: 9:400/759 of query aligns to 2:373/373 of 2haeB
- active site: Y31 (= Y39), A67 (= A75), K86 (= K94), E128 (= E136), D129 (= D137), D153 (= D161), D154 (= D162), N280 (= N288)
- binding nicotinamide-adenine-dinucleotide: T158 (= T166), N185 (≠ S193), G188 (= G196), A189 (= A197), A190 (= A198), D210 (= D220), R211 (≠ S221), V255 (≠ C263), S256 (= S264), R257 (≠ G265), L278 (= L286), A279 (= A287), N280 (= N288), N311 (= N320)
6ioxA Crystal structure of porphyromonas gingivalis phosphotransacetylase in complex with acetyl-coa (see paper)
35% identity, 43% coverage: 430:754/759 of query aligns to 7:334/339 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)
32% identity, 45% coverage: 416:757/759 of query aligns to 372:712/714 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)
32% identity, 43% coverage: 431:754/759 of query aligns to 3:324/325 of 1xcoD
2af3C Phosphotransacetylase from methanosarcina thermophila soaked with coenzyme a (see paper)
29% identity, 43% coverage: 430:757/759 of query aligns to 3:330/332 of 2af3C
- binding coenzyme a: R86 (≠ M518), S127 (≠ Y560), L131 (≠ F564), V135 (≠ K568), L146 (≠ T579), A147 (= A580), G172 (≠ Y599), M173 (≠ V600), M173 (≠ V600), V174 (≠ N601), E175 (≠ D602), N278 (≠ R704), Y281 (= Y707), K282 (≠ N708), Q285 (vs. gap), G294 (= G721), P295 (= P722), T297 (≠ L724), D306 (≠ V733), L307 (= L734), S308 (≠ T735)
P38503 Phosphate acetyltransferase; Phosphotransacetylase; EC 2.3.1.8 from Methanosarcina thermophila (see 2 papers)
29% identity, 43% coverage: 430:757/759 of query aligns to 4:331/333 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
1gq2A Malic enzyme from pigeon liver (see paper)
26% identity, 45% coverage: 69:407/759 of query aligns to 137:516/555 of 1gq2A
- active site: R143 (≠ A75), K161 (= K94), E233 (= E136), D234 (= D137), D256 (= D161), D257 (= D162), N396 (= N288)
- binding manganese (ii) ion: K161 (= K94), 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 (≠ S264), I370 (vs. gap), L394 (= L286), N396 (= N288), G440 (≠ V318), N441 (= N319), N442 (= N320)
- binding oxalate ion: R143 (≠ A75), L145 (= L77), D257 (= D162), N396 (= N288), N442 (= N320)
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)
26% identity, 45% coverage: 69:407/759 of query aligns to 138:517/557 of P40927
- D141 (≠ N72) mutation to N: Increases Km for manganese 14-fold. Increases Km for malate 5-fold.
- R144 (≠ A75) binding ; binding
- K162 (= K94) binding ; mutation to A: Decreases kcat 235-fold. no effect on Km for NADP.
- D194 (= D115) mutation to N: No effect on Km for manganese. Increases Km for malate 8-fold.
- E234 (= E136) binding
- D235 (= D137) binding
- N238 (≠ A140) binding
- D258 (= D162) binding
- AGEA 291:294 (≠ AGAA 195:198) binding
- S325 (= S221) binding
- K340 (= K237) mutation to A: Increases Km for NADP 65-fold. No effect on kcat.
- N397 (= N288) binding
- N443 (= N320) binding ; binding
- D464 (≠ E341) 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)
25% identity, 50% coverage: 60:439/759 of query aligns to 222:636/636 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 (≠ Q148) 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 (≠ M203) 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 (≠ L297) mutation to E: No effect on kcat and Km for NADP. Increases Km for malate 2-fold.
- L544 (≠ I327) 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.
6w49A Trypanosoma cruzi malic enzyme in complex with inhibitor (mec010) (see paper)
26% identity, 42% coverage: 35:351/759 of query aligns to 82:475/543 of 6w49A
6w59A Trypanosoma cruzi malic enzyme in complex with inhibitor (mec063) (see paper)
26% identity, 42% coverage: 35:351/759 of query aligns to 82:475/544 of 6w59A
- active site: Y86 (= Y39), R139 (≠ A75), K157 (= K94), E228 (= E136), D229 (= D137), D251 (= D161), D252 (= D162), N399 (= N288)
- binding 3,5-bis(fluoranyl)-~{N}-[3-[[4-(trifluoromethyloxy)phenyl]sulfamoyl]phenyl]benzamide: H99 (≠ K52), F102 (≠ L55), R103 (≠ K56), E104 (≠ A57)
6w56A Trypanosoma cruzi malic enzyme in complex with inhibitor (mec062) (see paper)
26% identity, 42% coverage: 35:351/759 of query aligns to 82:475/544 of 6w56A
- active site: Y86 (= Y39), R139 (≠ A75), K157 (= K94), E228 (= E136), D229 (= D137), D251 (= D161), D252 (= D162), N399 (= N288)
- binding ~{N}-[3-[[4-[bis(fluoranyl)methoxy]phenyl]sulfamoyl]phenyl]-3,5-bis(fluoranyl)benzamide: H99 (≠ K52), F102 (≠ L55), R103 (≠ K56)
Query Sequence
>16562 FitnessBrowser__Keio:16562
MDDQLKQSALDFHEFPVPGKIQVSPTKPLATQRDLALAYSPGVAAPCLEIEKDPLKAYKY
TARGNLVAVISNGTAVLGLGNIGALAGKPVMEGKGVLFKKFAGIDVFDIEVDELDPDKFI
EVVAALEPTFGGINLEDIKAPECFYIEQKLRERMNIPVFHDDQHGTAIISTAAILNGLRV
VEKNISDVRMVVSGAGAAAIACMNLLVALGLQKHNIVVCDSKGVIYQGREPNMAETKAAY
AVVDDGKRTLDDVIEGADIFLGCSGPKVLTQEMVKKMARAPMILALANPEPEILPPLAKE
VRPDAIICTGRSDYPNQVNNVLCFPFIFRGALDVGATAINEEMKLAAVRAIAELAHAEQS
EVVASAYGDQDLSFGPEYIIPKPFDPRLIVKIAPAVAKAAMESGVATRPIADFDVYIDKL
TEFVYKTNLFMKPIFSQARKAPKRVVLPEGEEARVLHATQELVTLGLAKPILIGRPNVIE
MRIQKLGLQIKAGVDFEIVNNESDPRFKEYWTEYFQIMKRRGVTQEQAQRALISNPTVIG
AIMVQRGEADAMICGTVGDYHEHFSVVKNVFGYRDGVHTAGAMNALLLPSGNTFIADTYV
NDEPDAEELAEITLMAAETVRRFGIEPRVALLSHSNFGSSDCPSSSKMRQALELVRERAP
ELMIDGEMHGDAALVEAIRNDRMPDSSLKGSANILVMPNMEAARISYNLLRVSSSEGVTV
GPVLMGVAKPVHVLTPIASVRRIVNMVALAVVEAQTQPL
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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