SitesBLAST
Comparing WP_003465338.1 NCBI__GCF_000359605.1:WP_003465338.1 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)
3d3fA Crystal structure of yvgn and cofactor NADPH from bacillus subtilis (see paper)
67% identity, 98% coverage: 4:276/279 of query aligns to 3:273/275 of 3d3fA
- active site: D48 (= D49), Y53 (= Y54), K78 (= K79), H111 (= H112)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G22 (= G23), F24 (= F25), D48 (= D49), Y53 (= Y54), H111 (= H112), S140 (= S143), N141 (= N144), Q162 (= Q165), W188 (= W191), S189 (= S192), P190 (= P193), L191 (= L194), Q193 (= Q196), L197 (= L200), I229 (= I232), K231 (= K234), S232 (= S235), K234 (= K237), R237 (= R240), E240 (= E243), N241 (= N244)
3b3dA B.Subtilis ytbe (see paper)
61% identity, 100% coverage: 1:278/279 of query aligns to 1:280/280 of 3b3dA
4g5dA X-ray crystal structure of prostaglandin f synthase from leishmania major friedlin bound to NADPH (see paper)
56% identity, 97% coverage: 6:275/279 of query aligns to 5:280/283 of 4g5dA
- active site: D48 (= D49), Y53 (= Y54), K78 (= K79), H111 (= H112)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G22 (= G23), V23 (= V24), W24 (≠ F25), D48 (= D49), Y53 (= Y54), H111 (= H112), S148 (= S143), N149 (= N144), Q170 (= Q165), W196 (= W191), S197 (= S192), P198 (= P193), L199 (= L194), Q201 (= Q196), G202 (= G197), L205 (= L200), I237 (= I232), P238 (= P233), K239 (= K234), S240 (= S235), V241 (= V236), H242 (≠ K237), R245 (= R240), E248 (= E243), N249 (= N244)
4gieA Crystal structure of prostaglandin f synthase from trypanosoma cruzi bound to NADP (see paper)
55% identity, 97% coverage: 7:276/279 of query aligns to 13:283/288 of 4gieA
- active site: D55 (= D49), Y60 (= Y54), K85 (= K79), H118 (= H112)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G29 (= G23), W31 (≠ F25), D55 (= D49), Y60 (= Y54), H118 (= H112), W119 (= W113), N148 (= N144), Q169 (= Q165), W195 (= W191), S196 (= S192), P197 (= P193), L198 (= L194), S200 (≠ Q196), L207 (= L200), A224 (= A217), I239 (= I232), P240 (= P233), K241 (= K234), S242 (= S235), R247 (= R240), E250 (= E243), N251 (= N244)
4fziA Crystal structure of prostaglandin f synthase from trypanosoma cruzi (see paper)
55% identity, 97% coverage: 7:276/279 of query aligns to 2:272/277 of 4fziA
Q9GV41 9,11-endoperoxide prostaglandin H2 reductase; Prostaglandin F2-alpha synthase; EC 1.1.1.- from Trypanosoma brucei brucei
52% identity, 97% coverage: 3:274/279 of query aligns to 1:270/276 of Q9GV41
1vbjA The crystal structure of prostaglandin f synthase from trypanosoma brucei
52% identity, 97% coverage: 3:274/279 of query aligns to 6:275/281 of 1vbjA
- active site: D52 (= D49), Y57 (= Y54), K82 (= K79), H115 (= H112)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G26 (= G23), M27 (≠ V24), W28 (≠ F25), D52 (= D49), Y57 (= Y54), H115 (= H112), N145 (= N144), Q166 (= Q165), W192 (= W191), S193 (= S192), P194 (= P193), L195 (= L194), Q197 (= Q196), G198 (= G197), V201 (≠ L200), A218 (= A217), I233 (= I232), K235 (= K234), S236 (= S235), G237 (≠ V236), R241 (= R240), E244 (= E243), N245 (= N244)
A0QV10 Aldo-keto reductase MSMEG_2408/MSMEI_2347; EC 1.1.1.- from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
53% identity, 97% coverage: 10:279/279 of query aligns to 6:274/275 of A0QV10
- K262 (≠ E267) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
3wbwA Crystal structure of gox0644 in complex with NADPH
44% identity, 96% coverage: 6:274/279 of query aligns to 3:267/271 of 3wbwA
- active site: D45 (= D49), Y50 (= Y54), K71 (= K79), H104 (= H112)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G20 (= G23), H104 (= H112), N136 (= N144), W183 (= W191), R184 (≠ S192), P185 (= P193), L186 (= L194), L192 (= L200), A209 (= A217), K226 (= K234), S227 (= S235), V228 (= V236), R232 (= R240), E235 (= E243), N236 (= N244)
2wzmA Crystal structure of a mycobacterium aldo-keto reductase in its apo and liganded form (see paper)
45% identity, 95% coverage: 8:273/279 of query aligns to 4:268/274 of 2wzmA
- active site: D44 (= D49), Y49 (= Y54), K74 (= K79), H107 (= H112)
- binding [(2r,3r,4r,5r)-5-(6-amino-9h-purin-9-yl)-3-hydroxy-4-(phosphonooxy)tetrahydrofuran-2-yl]methyl [(2r,3s,4s)-3,4-dihydroxytetrahydrofuran-2-yl]methyl dihydrogen diphosphate: Y186 (≠ W191), G187 (≠ S192), P188 (= P193), L189 (= L194), G190 (≠ K195), V191 (≠ Q196), G192 (= G197), L195 (= L200), A212 (= A217), I227 (= I232), R229 (≠ K234), S230 (= S235), R235 (= R240), N239 (= N244), R265 (≠ G270)
A0QV09 Aldo-keto reductase MSMEG_2407/MSMEI_2346; AKR; AKR5H1; EC 1.1.1.- from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
45% identity, 95% coverage: 8:273/279 of query aligns to 13:277/283 of A0QV09
- G196 (≠ S192) binding NADPH
- L198 (= L194) binding NADPH
- V200 (≠ Q196) binding NADPH
- I236 (= I232) binding NADPH
- R238 (≠ K234) binding NADPH
- S239 (= S235) binding NADPH
- A240 (≠ V236) binding NADPH
- R244 (= R240) binding NADPH
- S247 (≠ E243) binding NADPH
- N248 (= N244) binding NADPH
- R274 (≠ G270) binding NADPH
P51635 Aldo-keto reductase family 1 member A1; 3-DG-reducing enzyme; Alcohol dehydrogenase [NADP(+)]; Aldehyde reductase; Glucuronate reductase; Glucuronolactone reductase; S-nitroso-CoA reductase; ScorR; EC 1.1.1.2; EC 1.1.1.372; EC 1.1.1.54; EC 1.1.1.19; EC 1.1.1.20; EC 1.6.-.- from Rattus norvegicus (Rat) (see paper)
43% identity, 94% coverage: 7:268/279 of query aligns to 4:297/325 of P51635
- K13 (= K16) Not glycated
- K23 (= K26) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K30 (= K34) Not glycated
- K34 (= K38) Not glycated
- K61 (= K65) Not glycated
- K68 (vs. gap) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K80 (= K79) Not glycated
- K85 (≠ N84) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K97 (≠ T96) Not glycated
- K127 (vs. gap) Not glycated
- K134 (vs. gap) Not glycated
- K141 (= K122) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K145 (= K126) Not glycated
- K153 (≠ D134) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K157 (≠ R138) Not glycated
- K240 (≠ R211) Not glycated
- K257 (≠ E228) Not glycated
- K263 (= K234) Not glycated
- K287 (≠ D258) Not glycated
- K294 (= K265) Not glycated
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylthreonine
- 308 Not glycated
P14550 Aldo-keto reductase family 1 member A1; Alcohol dehydrogenase [NADP(+)]; Aldehyde reductase; Glucuronate reductase; Glucuronolactone reductase; S-nitroso-CoA reductase; ScorR; EC 1.1.1.2; EC 1.1.1.372; EC 1.1.1.54; EC 1.1.1.19; EC 1.1.1.20; EC 1.6.-.- from Homo sapiens (Human) (see 5 papers)
44% identity, 94% coverage: 7:268/279 of query aligns to 4:297/325 of P14550
- Y50 (= Y54) active site, Proton donor; mutation to A: Abolished reductase activity.; mutation to F: Complete loss of enzymatic activity.; mutation to H: Complete loss of enzymatic activity.
- N52 (= N56) to S: reduced activity towards daunorubicin; dbSNP:rs2229540
- E55 (≠ G59) to D: reduced activity towards daunorubicin; dbSNP:rs6690497
- K80 (= K79) Lowers pKa of active site Tyr; mutation to M: Complete loss of enzymatic activity.
- H113 (= H112) mutation to Q: Strong decrease in enzymatic activity.
- K127 (vs. gap) mutation to A: Abolished S-nitroso-CoA reductase activity without affecting ability to reduce S-nitrosoglutathione, glyceraldehyde or glucuronate.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 299 I→A: No change in enzymatic activity.; I→C: No change in enzymatic activity.
- 300 V→C: No change in enzymatic activity.
- 312 R→A: Abolished S-nitrosoglutathione reductase activity without affecting ability to reduce S-nitroso-CoA.
Q9JII6 Aldo-keto reductase family 1 member A1; Alcohol dehydrogenase [NADP(+)]; Aldehyde reductase; Glucuronate reductase; Glucuronolactone reductase; S-nitroso-CoA reductase; ScorR; EC 1.1.1.2; EC 1.1.1.372; EC 1.1.1.54; EC 1.1.1.19; EC 1.1.1.20; EC 1.6.-.- from Mus musculus (Mouse)
43% identity, 94% coverage: 7:268/279 of query aligns to 4:297/325 of Q9JII6
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylthreonine
3h4gA Structure of aldehyde reductase holoenzyme in complex with potent aldose reductase inhibitor fidarestat: implications for inhibitor binding and selectivity (see paper)
43% identity, 94% coverage: 7:268/279 of query aligns to 4:297/320 of 3h4gA
- active site: D45 (= D49), Y50 (= Y54), K80 (= K79), H113 (= H112)
- binding (2s,4s)-2-aminoformyl-6-fluoro-spiro[chroman-4,4'-imidazolidine]-2',5'-dione: W22 (≠ F25), Y50 (= Y54), H113 (= H112), W114 (= W113), W220 (vs. gap)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G23), T21 (≠ V24), W22 (≠ F25), D45 (= D49), Y50 (= Y54), H113 (= H112), S162 (= S143), N163 (= N144), Q184 (= Q165), Y210 (≠ W191), S211 (= S192), P212 (= P193), L213 (= L194), S215 (≠ Q196), D217 (≠ E198), A246 (= A217), I261 (= I232), P262 (= P233), K263 (= K234), S264 (= S235), V265 (= V236), T266 (≠ K237), R269 (= R240), Q272 (≠ E243), N273 (= N244)
Sites not aligning to the query:
3cv7A Crystal structure of porcine aldehyde reductase ternary complex (see paper)
43% identity, 94% coverage: 7:268/279 of query aligns to 4:297/322 of 3cv7A
- active site: D45 (= D49), Y50 (= Y54), K80 (= K79), H113 (= H112)
- binding 3,5-dichloro-2-hydroxybenzoic acid: W22 (≠ F25), Y50 (= Y54), W82 (= W81), H113 (= H112)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G23), T21 (≠ V24), W22 (≠ F25), Y50 (= Y54), H113 (= H112), Q184 (= Q165), Y210 (≠ W191), S211 (= S192), P212 (= P193), L213 (= L194), S215 (≠ Q196), A246 (= A217), I261 (= I232), P262 (= P233), K263 (= K234), S264 (= S235), V265 (= V236), T266 (≠ K237), R269 (= R240), Q272 (≠ E243), N273 (= N244)
Sites not aligning to the query:
3fx4A Porcine aldehyde reductase in ternary complex with inhibitor (see paper)
43% identity, 94% coverage: 7:268/279 of query aligns to 4:297/325 of 3fx4A
- active site: D45 (= D49), Y50 (= Y54), K80 (= K79), H113 (= H112)
- binding [(5Z)-5-{[3-(carboxymethoxy)-4-methoxyphenyl]methylidene}-2,4-dioxo-1,3-thiazolidin-3-yl]acetic acid: W22 (≠ F25), Y50 (= Y54), H113 (= H112), R218 (vs. gap), A219 (vs. gap)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G23), T21 (≠ V24), W22 (≠ F25), D45 (= D49), Y50 (= Y54), H113 (= H112), Q184 (= Q165), Y210 (≠ W191), S211 (= S192), P212 (= P193), L213 (= L194), S215 (≠ Q196), A246 (= A217), I261 (= I232), P262 (= P233), K263 (= K234), S264 (= S235), V265 (= V236), T266 (≠ K237), R269 (= R240), Q272 (≠ E243), N273 (= N244)
Sites not aligning to the query:
P50578 Aldo-keto reductase family 1 member A1; Alcohol dehydrogenase [NADP(+)]; Aldehyde reductase; Glucuronate reductase; Glucuronolactone reductase; S-nitroso-CoA reductase; ScorR; EC 1.1.1.2; EC 1.1.1.372; EC 1.1.1.54; EC 1.1.1.19; EC 1.1.1.20; EC 1.6.-.- from Sus scrofa (Pig) (see 2 papers)
43% identity, 94% coverage: 7:268/279 of query aligns to 4:297/325 of P50578
- T21 (≠ V24) binding NADP(+)
- W22 (≠ F25) binding NADP(+)
- D45 (= D49) binding NADP(+)
- Y50 (= Y54) active site, Proton donor; mutation to F: Abolished aldo-keto reductase activity.
- S162 (= S143) binding NADP(+)
- N163 (= N144) binding NADP(+)
- S211 (= S192) binding NADP(+)
- L213 (= L194) binding NADP(+)
- S215 (≠ Q196) binding NADP(+)
- S216 (≠ G197) binding NADP(+)
- K263 (= K234) binding NADP(+)
- S264 (= S235) binding NADP(+)
- V265 (= V236) binding NADP(+)
- T266 (≠ K237) binding NADP(+)
- R269 (= R240) binding NADP(+)
- Q272 (≠ E243) binding NADP(+)
- N273 (= N244) binding NADP(+)
1vp5A Crystal structure of 2,5-diketo-d-gluconic acid reductase (tm1009) from thermotoga maritima at 2.40 a resolution
46% identity, 93% coverage: 9:267/279 of query aligns to 5:265/284 of 1vp5A
- active site: D44 (= D49), Y49 (= Y54), K78 (= K79), H111 (= H112)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G23), V20 (= V24), F21 (= F25), D44 (= D49), Y49 (= Y54), N140 (= N144), Q161 (= Q165), W187 (= W191), G188 (≠ S192), P189 (= P193), F190 (≠ L194), E192 (≠ Q196), F198 (≠ L200), A215 (= A217), I230 (= I232), K232 (= K234), T233 (≠ S235), V234 (= V236), R238 (= R240), E241 (= E243), N242 (= N244)
P06632 2,5-diketo-D-gluconic acid reductase A; 2,5-DKG reductase A; 2,5-DKGR A; 25DKGR-A; AKR5C; EC 1.1.1.346 from Corynebacterium sp. (strain ATCC 31090) (see 3 papers)
44% identity, 97% coverage: 8:277/279 of query aligns to 5:278/278 of P06632
- Y50 (= Y54) active site, Proton donor
- H108 (= H112) binding substrate
- 188:242 (vs. 192:244, 48% identical) binding NADP(+)
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
Query Sequence
>WP_003465338.1 NCBI__GCF_000359605.1:WP_003465338.1
MTLNLQSTTTLHNGVKMPWFGLGVFKVQEGEEVKNSVKWALEHGYKHIDTAAAYKNEQGV
GEAIKESGIPREELFVTSKLWNGNQGYDETIAAFETTLQQLGMDYLDLYLIHWPVPEQNK
YKESWKAMEKLYHDGKIRAIGVSNFKEHHLDDLLQEADVVPMVNQVEYHPHLTQKSLHDY
CKKHQIQLEAWSPLKQGEILSEPVLKEIAERHGKSPAQVILRWDLQNEVVTIPKSVKQHR
IHENADVFDFELSQQEVDQLNQLNKDERVGPDPDEMNIT
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