SitesBLAST
Comparing WP_035702093.1 NCBI__GCF_000691145.1:WP_035702093.1 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)
3b3dA B.Subtilis ytbe (see paper)
72% identity, 99% coverage: 4:279/279 of query aligns to 5:280/280 of 3b3dA
3d3fA Crystal structure of yvgn and cofactor NADPH from bacillus subtilis (see paper)
63% identity, 99% coverage: 4:279/279 of query aligns to 4:275/275 of 3d3fA
- active site: D48 (= D48), Y53 (= Y53), K78 (= K82), H111 (= H115)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G22 (= G22), F24 (= F24), D48 (= D48), Y53 (= Y53), H111 (= H115), S140 (= S144), N141 (= N145), Q162 (= Q166), W188 (= W192), S189 (= S193), P190 (= P194), L191 (= L195), Q193 (= Q197), L197 (= L201), I229 (= I233), K231 (= K235), S232 (= S236), K234 (= K238), R237 (= R241), E240 (= E244), N241 (= N245)
4gieA Crystal structure of prostaglandin f synthase from trypanosoma cruzi bound to NADP (see paper)
53% identity, 99% coverage: 1:277/279 of query aligns to 8:283/288 of 4gieA
- active site: D55 (= D48), Y60 (= Y53), K85 (= K82), H118 (= H115)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G29 (= G22), W31 (≠ F24), D55 (= D48), Y60 (= Y53), H118 (= H115), W119 (= W116), N148 (= N145), Q169 (= Q166), W195 (= W192), S196 (= S193), P197 (= P194), L198 (= L195), S200 (≠ Q197), L207 (= L201), A224 (= A218), I239 (= I233), P240 (= P234), K241 (= K235), S242 (= S236), R247 (= R241), E250 (= E244), N251 (= N245)
4fziA Crystal structure of prostaglandin f synthase from trypanosoma cruzi (see paper)
54% identity, 96% coverage: 9:277/279 of query aligns to 5:272/277 of 4fziA
4g5dA X-ray crystal structure of prostaglandin f synthase from leishmania major friedlin bound to NADPH (see paper)
53% identity, 97% coverage: 9:279/279 of query aligns to 9:283/283 of 4g5dA
- active site: D48 (= D48), Y53 (= Y53), K78 (= K82), H111 (= H115)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G22 (= G22), V23 (= V23), W24 (≠ F24), D48 (= D48), Y53 (= Y53), H111 (= H115), S148 (= S144), N149 (= N145), Q170 (= Q166), W196 (= W192), S197 (= S193), P198 (= P194), L199 (= L195), Q201 (= Q197), G202 (= G198), L205 (= L201), I237 (= I233), P238 (= P234), K239 (= K235), S240 (= S236), V241 (≠ T237), H242 (≠ K238), R245 (= R241), E248 (= E244), N249 (= N245)
Q9GV41 9,11-endoperoxide prostaglandin H2 reductase; Prostaglandin F2-alpha synthase; EC 1.1.1.- from Trypanosoma brucei brucei
50% identity, 98% coverage: 4:277/279 of query aligns to 3:272/276 of Q9GV41
1vbjA The crystal structure of prostaglandin f synthase from trypanosoma brucei
50% identity, 98% coverage: 4:277/279 of query aligns to 8:277/281 of 1vbjA
- active site: D52 (= D48), Y57 (= Y53), K82 (= K82), H115 (= H115)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G26 (= G22), M27 (≠ V23), W28 (≠ F24), D52 (= D48), Y57 (= Y53), H115 (= H115), N145 (= N145), Q166 (= Q166), W192 (= W192), S193 (= S193), P194 (= P194), L195 (= L195), Q197 (= Q197), G198 (= G198), V201 (≠ L201), A218 (= A218), I233 (= I233), K235 (= K235), S236 (= S236), G237 (≠ T237), R241 (= R241), E244 (= E244), N245 (= N245)
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)
49% identity, 97% coverage: 9:279/279 of query aligns to 6:273/275 of A0QV10
- K262 (= K268) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
1vp5A Crystal structure of 2,5-diketo-d-gluconic acid reductase (tm1009) from thermotoga maritima at 2.40 a resolution
50% identity, 93% coverage: 9:268/279 of query aligns to 6:265/284 of 1vp5A
- active site: D44 (= D48), Y49 (= Y53), K78 (= K82), H111 (= H115)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G22), V20 (= V23), F21 (= F24), D44 (= D48), Y49 (= Y53), N140 (= N145), Q161 (= Q166), W187 (= W192), G188 (≠ S193), P189 (= P194), F190 (≠ L195), E192 (≠ Q197), F198 (≠ L201), A215 (= A218), I230 (= I233), K232 (= K235), T233 (≠ S236), V234 (≠ T237), R238 (= R241), E241 (= E244), N242 (= N245)
3wbwA Crystal structure of gox0644 in complex with NADPH
42% identity, 99% coverage: 3:279/279 of query aligns to 1:271/271 of 3wbwA
- active site: D45 (= D48), Y50 (= Y53), K71 (= K82), H104 (= H115)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G20 (= G22), H104 (= H115), N136 (= N145), W183 (= W192), R184 (≠ S193), P185 (= P194), L186 (= L195), L192 (= L201), A209 (= A218), K226 (= K235), S227 (= S236), V228 (≠ T237), R232 (= R241), E235 (= E244), N236 (= N245)
3cv7A Crystal structure of porcine aldehyde reductase ternary complex (see paper)
40% identity, 95% coverage: 6:270/279 of query aligns to 4:298/322 of 3cv7A
- active site: D45 (= D48), Y50 (= Y53), K80 (= K82), H113 (= H115)
- binding 3,5-dichloro-2-hydroxybenzoic acid: W22 (≠ F24), Y50 (= Y53), W82 (= W84), H113 (= H115)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G22), T21 (≠ V23), W22 (≠ F24), Y50 (= Y53), H113 (= H115), Q184 (= Q166), Y210 (≠ W192), S211 (= S193), P212 (= P194), L213 (= L195), S215 (≠ Q197), A246 (= A218), I261 (= I233), P262 (= P234), K263 (= K235), S264 (= S236), V265 (≠ T237), T266 (≠ K238), R269 (= R241), Q272 (≠ E244), N273 (= N245)
Sites not aligning to the query:
3h4gA Structure of aldehyde reductase holoenzyme in complex with potent aldose reductase inhibitor fidarestat: implications for inhibitor binding and selectivity (see paper)
40% identity, 95% coverage: 6:270/279 of query aligns to 4:298/320 of 3h4gA
- active site: D45 (= D48), Y50 (= Y53), K80 (= K82), H113 (= H115)
- binding (2s,4s)-2-aminoformyl-6-fluoro-spiro[chroman-4,4'-imidazolidine]-2',5'-dione: W22 (≠ F24), Y50 (= Y53), H113 (= H115), W114 (= W116), W220 (vs. gap)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G22), T21 (≠ V23), W22 (≠ F24), D45 (= D48), Y50 (= Y53), H113 (= H115), S162 (= S144), N163 (= N145), Q184 (= Q166), Y210 (≠ W192), S211 (= S193), P212 (= P194), L213 (= L195), S215 (≠ Q197), D217 (≠ E199), A246 (= A218), I261 (= I233), P262 (= P234), K263 (= K235), S264 (= S236), V265 (≠ T237), T266 (≠ K238), R269 (= R241), Q272 (≠ E244), N273 (= N245)
Sites not aligning to the query:
3fx4A Porcine aldehyde reductase in ternary complex with inhibitor (see paper)
40% identity, 95% coverage: 6:270/279 of query aligns to 4:298/325 of 3fx4A
- active site: D45 (= D48), Y50 (= Y53), K80 (= K82), H113 (= H115)
- binding [(5Z)-5-{[3-(carboxymethoxy)-4-methoxyphenyl]methylidene}-2,4-dioxo-1,3-thiazolidin-3-yl]acetic acid: W22 (≠ F24), Y50 (= Y53), H113 (= H115), R218 (vs. gap), A219 (vs. gap), F298 (≠ I270)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G22), T21 (≠ V23), W22 (≠ F24), D45 (= D48), Y50 (= Y53), H113 (= H115), Q184 (= Q166), Y210 (≠ W192), S211 (= S193), P212 (= P194), L213 (= L195), S215 (≠ Q197), A246 (= A218), I261 (= I233), P262 (= P234), K263 (= K235), S264 (= S236), V265 (≠ T237), T266 (≠ K238), R269 (= R241), Q272 (≠ E244), N273 (= N245)
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)
40% identity, 95% coverage: 6:270/279 of query aligns to 4:298/325 of P50578
- T21 (≠ V23) binding NADP(+)
- W22 (≠ F24) binding NADP(+)
- D45 (= D48) binding NADP(+)
- Y50 (= Y53) active site, Proton donor; mutation to F: Abolished aldo-keto reductase activity.
- S162 (= S144) binding NADP(+)
- N163 (= N145) binding NADP(+)
- S211 (= S193) binding NADP(+)
- L213 (= L195) binding NADP(+)
- S215 (≠ Q197) binding NADP(+)
- S216 (≠ G198) binding NADP(+)
- K263 (= K235) binding NADP(+)
- S264 (= S236) binding NADP(+)
- V265 (≠ T237) binding NADP(+)
- T266 (≠ K238) binding NADP(+)
- R269 (= R241) binding NADP(+)
- Q272 (≠ E244) binding NADP(+)
- N273 (= N245) binding NADP(+)
5jh2A Crystal structure of the holo form of akr4c7 from maize (see paper)
42% identity, 92% coverage: 9:266/279 of query aligns to 5:256/257 of 5jh2A
- active site: D43 (= D48), Y48 (= Y53), K77 (= K82), H110 (= H115)
- binding adenosine-2'-5'-diphosphate: S185 (= S193), P186 (= P194), L187 (= L195), G188 (= G198), A208 (= A218), K225 (= K235), S226 (= S236), T227 (= T237), R231 (= R241), N235 (= N245)
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)
40% identity, 95% coverage: 6:269/279 of query aligns to 4:297/325 of P14550
- Y50 (= Y53) 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 (= N55) to S: reduced activity towards daunorubicin; dbSNP:rs2229540
- E55 (≠ G58) to D: reduced activity towards daunorubicin; dbSNP:rs6690497
- K80 (= K82) Lowers pKa of active site Tyr; mutation to M: Complete loss of enzymatic activity.
- H113 (= H115) 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.
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)
40% identity, 95% coverage: 6:269/279 of query aligns to 4:297/325 of P51635
- K13 (≠ R15) Not glycated
- K23 (≠ Q25) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K30 (≠ I33) Not glycated
- K34 (= K37) Not glycated
- K61 (≠ Q64) Not glycated
- K68 (≠ T70) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K80 (= K82) Not glycated
- K85 (≠ D87) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K97 (≠ D99) Not glycated
- K127 (vs. gap) Not glycated
- K134 (vs. gap) Not glycated
- K141 (= K123) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K145 (≠ R127) Not glycated
- K153 (≠ E135) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K157 (≠ R139) Not glycated
- K240 (≠ T212) Not glycated
- K257 (≠ G229) Not glycated
- K263 (= K235) Not glycated
- K287 (= K259) Not glycated
- K294 (≠ E266) Not glycated
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylthreonine
- 308 Not glycated
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)
39% identity, 95% coverage: 6:269/279 of query aligns to 4:297/325 of Q9JII6
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylthreonine
O80944 Aldo-keto reductase family 4 member C8; EC 1.1.1.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
40% identity, 93% coverage: 10:268/279 of query aligns to 10:285/311 of O80944
3h7rA Crystal structure of the plant stress-response enzyme akr4c8 (see paper)
40% identity, 93% coverage: 10:268/279 of query aligns to 6:281/307 of 3h7rA
- active site: D39 (= D48), Y44 (= Y53), K73 (= K82), H106 (= H115)
- binding acetate ion: Y20 (≠ F24), Y44 (= Y53), H106 (= H115)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G22), T19 (≠ V23), Y20 (≠ F24), D39 (= D48), Y44 (= Y53), H106 (= H115), Q172 (= Q166), Y198 (≠ W192), S199 (= S193), P200 (= P194), L201 (= L195), S203 (vs. gap), Q204 (vs. gap), R210 (vs. gap), A231 (= A218), L246 (≠ I233), P247 (= P234), K248 (= K235), S249 (= S236), S250 (≠ T237), R254 (= R241), E257 (= E244), N258 (= N245)
Query Sequence
>WP_035702093.1 NCBI__GCF_000691145.1:WP_035702093.1
MNDLQSTKTLNNGVRMPGFGLGVFQVEEGTELIEAVKTAIQLGYRSIDTASIYGNEEGVG
RGIQLGLAETGLRREDIFVTSKVWNADLGYEATLKAYEDSLKKLQLDYLDLYLIHWPVEG
KYKEAWRALETLYREGKVRAIGVSNFQPHHLDELLTDADIIPAINQVEFHPKLTQETLFT
YLKTHGIQMEAWSPLMQGELLHHPLITELAGTYSKTPAQIILRWDVQKGVITIPKSTKAH
RLKENADIFDFVLSDEDMKRLSDLNENKRIGPDPDNFDF
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