SitesBLAST
Comparing WP_025274003.1 NCBI__GCF_000527155.1:WP_025274003.1 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)
Q7Z5P4 17-beta-hydroxysteroid dehydrogenase 13; 17-beta-HSD 13; Hepatic retinol/retinal dehydrogenase; Short chain dehydrogenase/reductase family 16C member 3; Short-chain dehydrogenase/reductase 9; EC 1.1.1.-; EC 1.1.1.62; EC 1.1.1.105 from Homo sapiens (Human) (see 2 papers)
37% identity, 33% coverage: 317:513/590 of query aligns to 28:227/300 of Q7Z5P4
- GIG 47:49 (= GIG 336:338) mutation to AIA: Loss of retinol/retinal dehydrogenase activity.
- 69:84 (vs. 358:370, 38% identical) mutation Missing: Does not localize to lipid droplets.
- 85:93 (vs. 371:382, 33% identical) mutation Missing: Does not localize to lipid droplets.
- 94:106 (vs. 383:395, 23% identical) mutation Missing: Does not localize to lipid droplets.
- R97 (≠ F386) mutation to A: Decreased retinol/retinal dehydrogenase activity; when associated with A-101.
- Y101 (≠ Q390) mutation to A: Decreased retinol/retinal dehydrogenase activity; when associated with A-97.
- N144 (= N433) mutation to A: Loss of retinol/retinal dehydrogenase activity.
- K153 (= K442) mutation to A: Loss of retinol/retinal dehydrogenase activity; when associated with A-156.
- L156 (≠ A445) mutation to A: Loss of retinol/retinal dehydrogenase activity; when associated with A-153.
- S172 (= S461) mutation to A: Loss of retinol/retinal dehydrogenase activity.
- Y185 (= Y474) mutation to A: Loss of retinol/retinal dehydrogenase activity; when associated with A-189.
- K189 (= K478) mutation to A: Loss of retinol/retinal dehydrogenase activity; when associated with A-185.
- L199 (= L488) mutation to A: Loss of retinol/retinal dehydrogenase activity; when associated with A-202.
- E202 (= E491) mutation to A: Loss of retinol/retinal dehydrogenase activity; when associated with A-199.
- K208 (≠ P494) mutation to A: Decreased retinol/retinal dehydrogenase activity.
Sites not aligning to the query:
- 22:28 mutation Missing: Does not localize to lipid droplets.
- 260 P → S: loss of retinol/retinal dehydrogenase activity; does not affect localization to lipid droplets; dbSNP:rs62305723
8g84A Crystal structures of hsd17b13 complexes (see paper)
34% identity, 35% coverage: 309:513/590 of query aligns to 19:226/297 of 8g84A
- binding nicotinamide-adenine-dinucleotide: G42 (= G332), H45 (≠ S335), G46 (= G336), I47 (= I337), D66 (= D356), I67 (= I357), V91 (= V381), C93 (≠ V383), N119 (= N409), G121 (= G411), I142 (≠ V432), V169 (= V459), S171 (= S461), Y184 (= Y474), K188 (= K478), P217 (= P504), V220 (= V507), T222 (= T509), F224 (≠ I511)
8g89A Hsd17b13 in complex with cofactor and inhibitor (see paper)
34% identity, 35% coverage: 309:513/590 of query aligns to 19:226/285 of 8g89A
- binding nicotinamide-adenine-dinucleotide: G42 (= G332), H45 (≠ S335), G46 (= G336), I47 (= I337), D66 (= D356), I67 (= I357), V91 (= V381), D92 (≠ N382), C93 (≠ V383), N119 (= N409), A120 (= A410), G121 (= G411), I142 (≠ V432), S171 (= S461), Y184 (= Y474), K188 (= K478), P217 (= P504), V218 (≠ G505), F219 (= F506), V220 (= V507), T222 (= T509), F224 (≠ I511)
- binding 3-fluoro-N-({(1r,4r)-4-[(2-fluorophenoxy)methyl]-1-hydroxycyclohexyl}methyl)-4-hydroxybenzamide: S171 (= S461), C173 (≠ A463), I178 (≠ V468), P179 (≠ R469), Y180 (≠ I470), Y184 (= Y474), F219 (= F506), T225 (= T512), K226 (≠ Q513)
Sites not aligning to the query:
8g9vE Crystal structures of 17-beta-hydroxysteroid dehydrogenase 13 (see paper)
36% identity, 33% coverage: 317:513/590 of query aligns to 28:227/293 of 8g9vE
- binding nicotinamide-adenine-dinucleotide: G43 (= G332), H46 (≠ S335), G47 (= G336), I48 (= I337), D67 (= D356), I68 (= I357), D93 (≠ N382), C94 (≠ V383), N120 (= N409), A121 (= A410), G122 (= G411), V170 (= V459), S172 (= S461), Y185 (= Y474), K189 (= K478), P218 (= P504), F220 (= F506), V221 (= V507), T223 (= T509), F225 (≠ I511)
- binding 4-{[2,5-dimethyl-3-(4-methylbenzene-1-sulfonyl)benzene-1-sulfonyl]amino}benzoic acid: S172 (= S461), V173 (≠ A462), C174 (≠ A463), I179 (≠ V468), Y185 (= Y474), V219 (≠ G505), F220 (= F506), F225 (≠ I511)
Sites not aligning to the query:
9av5A Hydroxysteroid 17-beta dehydrogenase 13
34% identity, 35% coverage: 309:513/590 of query aligns to 7:214/260 of 9av5A
- binding 8-(3,4-dichlorobenzene-1-sulfonamido)quinoline-5-carboxylic acid: S159 (= S461), V160 (≠ A462), E164 (≠ S466), I166 (≠ V468), L169 (= L471), Y172 (= Y474), V206 (≠ G505), F207 (= F506), T213 (= T512)
- binding nicotinamide-adenine-dinucleotide: G30 (= G332), H33 (≠ S335), G34 (= G336), I35 (= I337), D54 (= D356), I55 (= I357), V79 (= V381), D80 (≠ N382), C81 (≠ V383), N107 (= N409), G109 (= G411), I130 (≠ V432), V157 (= V459), A158 (= A460), S159 (= S461), Y172 (= Y474), K176 (= K478), P205 (= P504), F207 (= F506), V208 (= V507), T210 (= T509), F212 (≠ I511)
Sites not aligning to the query:
9av4A Hydroxysteroid 17-beta dehydrogenase 13
34% identity, 35% coverage: 309:513/590 of query aligns to 7:214/258 of 9av4A
- binding 4-(3,4-dichlorobenzene-1-sulfonamido)-2-fluorobenzoic acid: S159 (= S461), V160 (≠ A462), C161 (≠ A463), I166 (≠ V468), Y172 (= Y474), F207 (= F506)
- binding nicotinamide-adenine-dinucleotide: G30 (= G332), H33 (≠ S335), G34 (= G336), I35 (= I337), D54 (= D356), I55 (= I357), V79 (= V381), D80 (≠ N382), C81 (≠ V383), N107 (= N409), A108 (= A410), G109 (= G411), I130 (≠ V432), V157 (= V459), A158 (= A460), S159 (= S461), Y172 (= Y474), K176 (= K478), P205 (= P504), F207 (= F506), V208 (= V507), T210 (= T509), F212 (≠ I511)
Sites not aligning to the query:
9av8A Hydroxysteroid 17-beta dehydrogenase 13
34% identity, 35% coverage: 309:513/590 of query aligns to 20:227/271 of 9av8A
- binding 7-[3-chloro-4-(cyclobutylmethoxy)benzene-1-sulfonamido]-2-methyl-2H-indazole-4-carboxylic acid: S172 (= S461), V173 (≠ A462), E177 (≠ S466), L182 (= L471), Y185 (= Y474), V219 (≠ G505), F220 (= F506), F225 (≠ I511), T226 (= T512)
- binding nicotinamide-adenine-dinucleotide: G43 (= G332), H46 (≠ S335), G47 (= G336), I48 (= I337), D67 (= D356), I68 (= I357), V92 (= V381), C94 (≠ V383), N120 (= N409), A121 (= A410), G122 (= G411), I143 (≠ V432), S172 (= S461), Y185 (= Y474), K189 (= K478), P218 (= P504), V219 (≠ G505), V221 (= V507), T223 (= T509), F225 (≠ I511)
Sites not aligning to the query:
1yb1B Crystal structure of human 17-beta-hydroxysteroid dehydrogenase type xi
36% identity, 33% coverage: 319:513/590 of query aligns to 1:196/242 of 1yb1B
4yaiB Crystal structure of ligl in complex with nadh and gge from sphingobium sp. Strain syk-6 (see paper)
32% identity, 40% coverage: 325:561/590 of query aligns to 5:249/273 of 4yaiB
- active site: S144 (= S461), Y158 (= Y474), K162 (= K478), P203 (vs. gap)
- binding (1S,2R)-1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol: D95 (≠ A413), S144 (= S461), M151 (≠ V468), M155 (≠ L471), Y158 (= Y474), P188 (= P504), G189 (= G505), R222 (≠ K534), W228 (≠ G540)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G12 (= G332), S15 (= S335), G16 (= G336), I17 (= I337), D36 (= D356), I37 (= I357), H41 (≠ G361), L63 (≠ V381), D64 (≠ N382), V65 (= V383), N91 (= N409), A92 (= A410), G93 (= G411), T142 (≠ V459), S144 (= S461), Y158 (= Y474), K162 (= K478), P188 (= P504), G189 (= G505), P190 (≠ F506), I191 (≠ V507), S193 (≠ T509), R194 (≠ N510), I195 (= I511)
Sites not aligning to the query:
4yaiA Crystal structure of ligl in complex with nadh and gge from sphingobium sp. Strain syk-6 (see paper)
32% identity, 40% coverage: 325:561/590 of query aligns to 5:249/273 of 4yaiA
- active site: S144 (= S461), Y158 (= Y474), K162 (= K478), P203 (vs. gap)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G12 (= G332), S15 (= S335), G16 (= G336), I17 (= I337), D36 (= D356), I37 (= I357), R38 (≠ N358), H41 (≠ G361), L63 (≠ V381), D64 (≠ N382), V65 (= V383), N91 (= N409), A92 (= A410), G93 (= G411), I94 (= I412), T142 (≠ V459), S144 (= S461), Y158 (= Y474), K162 (= K478), P188 (= P504), G189 (= G505), P190 (≠ F506), I191 (≠ V507), S193 (≠ T509), R194 (≠ N510), I195 (= I511)
2cfcA Structural basis for stereo selectivity in the (r)- and (s)- hydroxypropylethane thiosulfonate dehydrogenases (see paper)
37% identity, 32% coverage: 326:513/590 of query aligns to 3:194/250 of 2cfcA
- active site: G13 (= G336), S142 (= S461), Y155 (= Y474), K159 (= K478)
- binding (2-[2-ketopropylthio]ethanesulfonate: F149 (≠ V468), R152 (≠ L471), Y155 (= Y474)
- binding nicotinamide-adenine-dinucleotide: G9 (= G332), S12 (= S335), G13 (= G336), N14 (≠ I337), D33 (= D356), L34 (≠ I357), A59 (vs. gap), D60 (≠ N382), V61 (= V383), N87 (= N409), A88 (= A410), G89 (= G411), I140 (≠ V459), P185 (= P504), G186 (= G505), M187 (≠ F506), I188 (≠ V507), T190 (= T509), P191 (≠ N510), M192 (≠ I511), T193 (= T512)
Sites not aligning to the query:
Q56840 2-(R)-hydroxypropyl-CoM dehydrogenase; R-HPCDH; 2-[(R)-2-hydroxypropylthio]ethanesulfonate dehydrogenase; Aliphatic epoxide carboxylation component III; Epoxide carboxylase component III; RHPCDH1; EC 1.1.1.268 from Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2) (see 4 papers)
37% identity, 32% coverage: 326:513/590 of query aligns to 3:194/250 of Q56840
- SGN 12:14 (≠ SGI 335:337) binding NAD(+)
- D33 (= D356) binding NAD(+)
- DV 60:61 (≠ NV 382:383) binding NAD(+)
- N87 (= N409) binding NAD(+)
- S142 (= S461) mutation to A: Retains weak activity. 120-fold decrease in kcat.; mutation to C: Loss of activity.
- R152 (≠ L471) binding 2-oxopropyl-coenzyme M; mutation to A: Almost loss of activity with the natural substrate 2-KPC, but does not affect activity with 2-butanone as substrate.
- Y155 (= Y474) mutation Y->E,F: Loss of activity.
- K159 (= K478) mutation to A: Loss of activity.
- R179 (≠ S498) mutation to A: Loss of activity.
- IETPM 188:192 (≠ VSTNI 507:511) binding NAD(+)
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 195:196 binding 2-oxopropyl-coenzyme M
- 196 R→A: Almost loss of activity with the natural substrate 2-KPC, but does not affect activity with 2-butanone as substrate.
- 203 R→A: Slight decrease in catalytic efficiency.
- 209 R→A: Does not affect catalytic efficiency.
8y83A Crystal structure of a ketoreductase from sphingobacterium siyangense sy1 with co-enzyme
35% identity, 31% coverage: 326:509/590 of query aligns to 7:191/249 of 8y83A
- binding nicotinamide-adenine-dinucleotide: G13 (= G332), S16 (= S335), G17 (= G336), I18 (= I337), D37 (= D356), I38 (= I357), A62 (≠ V381), D63 (≠ N382), S64 (≠ V383), N90 (= N409), M141 (≠ V459), Y156 (= Y474), K160 (= K478), P186 (= P504), G187 (= G505), Y188 (≠ F506), I189 (≠ V507)
Sites not aligning to the query:
4urfB Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
31% identity, 40% coverage: 323:559/590 of query aligns to 3:231/248 of 4urfB
- active site: G16 (= G336), S142 (= S461), I152 (≠ L471), Y155 (= Y474), K159 (= K478)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: L210 (≠ I538), R211 (≠ K539), R212 (≠ G540)
- binding bicarbonate ion: I92 (= I412), G94 (= G416), R109 (≠ Q428), R179 (≠ S498), S228 (≠ K556)
- binding nicotinamide-adenine-dinucleotide: G12 (= G332), G14 (= G334), N15 (≠ S335), G16 (= G336), I17 (= I337), D36 (= D356), I37 (= I357), D62 (≠ N382), T63 (≠ V383), N89 (= N409), A90 (= A410), G91 (= G411), I140 (≠ V459), Y155 (= Y474), K159 (= K478), P185 (= P504), A186 (≠ G505), I188 (≠ V507), T190 (= T509)
4urfA Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
31% identity, 40% coverage: 323:559/590 of query aligns to 3:231/248 of 4urfA
- active site: G16 (= G336), S142 (= S461), I152 (≠ L471), Y155 (= Y474), K159 (= K478)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: I92 (= I412), S93 (= S415), G94 (= G416), E95 (≠ A417), T97 (≠ L419), E101 (≠ D420), T103 (≠ P422), Q106 (≠ R425), R109 (≠ Q428), S175 (≠ P494), G177 (≠ D496)
- binding nicotinamide-adenine-dinucleotide: G12 (= G332), G14 (= G334), N15 (≠ S335), G16 (= G336), I17 (= I337), D36 (= D356), I37 (= I357), W41 (≠ G361), D62 (≠ N382), T63 (≠ V383), N89 (= N409), A90 (= A410), G91 (= G411), I140 (≠ V459), Y155 (= Y474), K159 (= K478), P185 (= P504), I188 (≠ V507), T190 (= T509)
Sites not aligning to the query:
4ureB Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
31% identity, 40% coverage: 323:559/590 of query aligns to 3:231/248 of 4ureB
- active site: G16 (= G336), S142 (= S461), I152 (≠ L471), Y155 (= Y474), K159 (= K478)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: N15 (≠ S335), G16 (= G336), I17 (= I337), N89 (= N409), G91 (= G411), Y155 (= Y474), P185 (= P504), A186 (≠ G505)
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
33% identity, 34% coverage: 323:521/590 of query aligns to 3:202/247 of 4jroC
- active site: G16 (= G336), S142 (= S461), Q152 (≠ L471), Y155 (= Y474), K159 (= K478)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G332), S14 (≠ G334), R15 (≠ S335), G16 (= G336), I17 (= I337), N35 (= N358), Y36 (≠ I359), N37 (≠ D360), G38 (= G361), S39 (vs. gap), N63 (= N382), V64 (= V383), N90 (= N409), A91 (= A410), I93 (= I412), I113 (≠ V432), S142 (= S461), Y155 (= Y474), K159 (= K478), P185 (= P504), I188 (≠ V507), T190 (= T509)
6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
33% identity, 34% coverage: 323:521/590 of query aligns to 3:202/248 of 6ixmC