SitesBLAST
Comparing CCNA_02178 CCNA_02178 short-chain alcohol dehydrogenase 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)
1gz6A (3r)-hydroxyacyl-coa dehydrogenase fragment of rat peroxisomal multifunctional enzyme type 2 (see paper)
50% identity, 91% coverage: 4:276/301 of query aligns to 3:275/301 of 1gz6A
- active site: S149 (= S153), Y162 (= Y166), K166 (= K170)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G15), L19 (= L20), D38 (= D39), L39 (= L40), S73 (= S74), V74 (= V75), N97 (= N101), A98 (= A102), G99 (= G103), I100 (= I104), H121 (= H125), T147 (= T151), S149 (= S153), Y162 (= Y166), K166 (= K170), P192 (= P196), A194 (= A198), S196 (≠ T200), R197 (= R201), M198 (= M202)
P97852 Peroxisomal multifunctional enzyme type 2; MFE-2; 17-beta-hydroxysteroid dehydrogenase 4; 17-beta-HSD 4; D-bifunctional protein; DBP; Multifunctional protein 2; MFP-2; EC 1.1.1.n12; EC 4.2.1.107; EC 4.2.1.119 from Rattus norvegicus (Rat) (see paper)
49% identity, 91% coverage: 2:276/301 of query aligns to 3:277/735 of P97852
- 16:40 (vs. 15:39, 76% identical) binding
P96825 Putative short-chain type dehydrogenase/reductase Rv0148; EC 1.1.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
48% identity, 91% coverage: 9:282/301 of query aligns to 7:280/286 of P96825
- K280 (= K282) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
1zbqA Crystal structure of human 17-beta-hydroxysteroid dehydrogenase type 4 in complex with NAD
46% identity, 91% coverage: 4:276/301 of query aligns to 3:275/302 of 1zbqA
- active site: S149 (= S153), Y162 (= Y166), K166 (= K170)
- binding nicotinamide-adenine-dinucleotide: G14 (= G15), G18 (= G19), L19 (= L20), D38 (= D39), L39 (= L40), S73 (= S74), V74 (= V75), N97 (= N101), A98 (= A102), T147 (= T151), S149 (= S153), Y162 (= Y166), K166 (= K170), P192 (= P196), N193 (≠ V197), A194 (= A198), S196 (≠ T200), R197 (= R201), M198 (= M202)
P51659 Peroxisomal multifunctional enzyme type 2; MFE-2; 17-beta-hydroxysteroid dehydrogenase 4; 17-beta-HSD 4; D-bifunctional protein; DBP; Multifunctional protein 2; MFP-2; Short chain dehydrogenase/reductase family 8C member 1; EC 1.1.1.n12; EC 4.2.1.107; EC 4.2.1.119 from Homo sapiens (Human) (see 5 papers)
45% identity, 91% coverage: 2:276/301 of query aligns to 3:277/736 of P51659
- G16 (= G15) to S: in DBPD; no dehydrogenase activity; dbSNP:rs137853096
- R106 (≠ K108) to H: in dbSNP:rs25640
Sites not aligning to the query:
- 347 Y→A: No hydratase activity.
- 366 E→A: No hydratase activity.
- 370 D→A: No effect.
- 406 H→A: No effect.
- 408 E→A: No effect.
- 410 Y→A: No effect.
- 457 N → Y: in DBPD; the mutation leads to an unstable protein; dbSNP:rs137853097
- 490 D→A: No effect.
- 505 Y→A: Completely inactive.
- 510 D→A: No hydratase activity.
- 511 W → R: in dbSNP:rs11539471
- 515 H→A: Completely inactive.
- 517 D→A: No effect.
- 532 H→A: No effect.
- 559 I → V: in dbSNP:rs11205
P22414 Peroxisomal hydratase-dehydrogenase-epimerase; HDE; Multifunctional beta-oxidation protein; MFP; EC 4.2.1.119; EC 1.1.1.n12 from Candida tropicalis (Yeast) (see paper)
46% identity, 94% coverage: 1:282/301 of query aligns to 1:281/906 of P22414
Sites not aligning to the query:
- 699 binding
- 700 binding
- 729 binding
- 757 binding
- 808 binding
- 810 binding
- 831 binding
- 856 binding
- 857 binding
- 858 binding
1gz6B (3r)-hydroxyacyl-coa dehydrogenase fragment of rat peroxisomal multifunctional enzyme type 2 (see paper)
47% identity, 91% coverage: 4:276/301 of query aligns to 3:252/278 of 1gz6B
- active site: S141 (= S153), Y154 (= Y166), K158 (= K170)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G15), L19 (= L20), D38 (= D39), L39 (= L40), S65 (= S74), V66 (= V75), N89 (= N101), A90 (= A102), G91 (= G103), H113 (= H125), T139 (= T151), S141 (= S153), Y154 (= Y166), K158 (= K170), P184 (= P196)
P73574 3-oxoacyl-[acyl-carrier-protein] reductase; 3-ketoacyl-acyl carrier protein reductase; EC 1.1.1.100 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
41% identity, 78% coverage: 6:239/301 of query aligns to 4:234/247 of P73574
- A14 (= A16) mutation to G: 4.2-fold increase in activity on acetoacetyl-CoA.
- P151 (≠ F161) mutation to F: 2.7-fold increase in activity on acetoacetyl-CoA.; mutation to V: 5.7-fold increase in activity on acetoacetyl-CoA.
- K160 (= K170) mutation to A: Almost no activity on acetoacetyl-CoA.
- F188 (≠ V197) mutation to Y: 3.3-fold increase in activity on acetoacetyl-CoA.
- N198 (≠ M207) mutation to R: 3.5-fold increase in activity on acetoacetyl-CoA.
1edoA The x-ray structure of beta-keto acyl carrier protein reductase from brassica napus complexed with NADP+ (see paper)
37% identity, 68% coverage: 10:215/301 of query aligns to 3:192/244 of 1edoA
- active site: G12 (= G19), S138 (= S153), Y151 (= Y166), K155 (= K170)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G15), S10 (≠ G17), R11 (≠ G18), I13 (≠ L20), N31 (= N38), Y32 (≠ S47), A33 (≠ G48), R34 (≠ G49), S35 (= S50), D59 (≠ S74), V60 (= V75), N86 (= N101), A87 (= A102), S138 (= S153), Y151 (= Y166), K155 (= K170), P181 (= P196), G182 (= G205), I184 (≠ M207), S186 (≠ P209), M188 (≠ V211)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
33% identity, 76% coverage: 5:232/301 of query aligns to 4:228/244 of 4nbuB
- active site: G18 (= G19), N111 (≠ H125), S139 (= S153), Q149 (= Q163), Y152 (= Y166), K156 (= K170)
- binding acetoacetyl-coenzyme a: D93 (= D107), K98 (= K112), S139 (= S153), N146 (= N160), V147 (≠ F161), Q149 (= Q163), Y152 (= Y166), F184 (≠ A198), M189 (≠ T203), K200 (= K214)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G15), N17 (≠ G18), G18 (= G19), I19 (≠ L20), D38 (= D39), F39 (≠ L40), V59 (≠ A63), D60 (≠ S74), V61 (= V75), N87 (= N101), A88 (= A102), G89 (= G103), I90 (= I104), T137 (= T151), S139 (= S153), Y152 (= Y166), K156 (= K170), P182 (= P196), F184 (≠ A198), T185 (≠ A199), T187 (≠ R201), M189 (≠ T203)
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
35% identity, 79% coverage: 6:243/301 of query aligns to 3:244/247 of 4jroC
- active site: G16 (= G19), S142 (= S153), Q152 (= Q163), Y155 (= Y166), K159 (= K170)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G15), S14 (≠ G17), R15 (≠ G18), G16 (= G19), I17 (≠ L20), N35 (= N38), Y36 (≠ S47), N37 (≠ G48), G38 (= G49), S39 (= S50), N63 (≠ S74), V64 (= V75), N90 (= N101), A91 (= A102), I93 (= I104), I113 (≠ V124), S142 (= S153), Y155 (= Y166), K159 (= K170), P185 (= P196), I188 (≠ A198), T190 (= T200)
6zzqA Crystal structure of (r)-3-hydroxybutyrate dehydrogenase from acinetobacter baumannii complexed with NAD+ and acetoacetate (see paper)
36% identity, 63% coverage: 6:196/301 of query aligns to 4:185/260 of 6zzqA
- active site: G17 (= G19), S142 (= S153), Y155 (= Y166)
- binding acetoacetic acid: Q94 (≠ L105), S142 (= S153), K152 (≠ Q163), Y155 (= Y166)
- binding nicotinamide-adenine-dinucleotide: G13 (= G15), S16 (≠ G18), G17 (= G19), I18 (≠ L20), D37 (= D39), M38 (≠ L40), D63 (≠ S74), V64 (= V75), N90 (= N101), A91 (= A102), G92 (= G103), M140 (≠ T151), A141 (≠ T152), S142 (= S153), Y155 (= Y166), K159 (= K170)
Sites not aligning to the query:
6zzsD Crystal structure of (r)-3-hydroxybutyrate dehydrogenase from acinetobacter baumannii complexed with NAD+ and 3-oxovalerate (see paper)
36% identity, 63% coverage: 6:196/301 of query aligns to 5:186/261 of 6zzsD
- active site: G18 (= G19), S143 (= S153), Y156 (= Y166)
- binding nicotinamide-adenine-dinucleotide: G14 (= G15), S17 (≠ G18), I19 (≠ L20), D38 (= D39), M39 (≠ L40), D64 (≠ S74), V65 (= V75), N91 (= N101), A92 (= A102), G93 (= G103), M141 (≠ T151), A142 (≠ T152), S143 (= S153), Y156 (= Y166), K160 (= K170), P186 (= P196)
- binding 3-oxidanylidenepentanoic acid: Q95 (≠ L105), S143 (= S153), N145 (≠ S155), K153 (≠ Q163), Y156 (= Y166)
Sites not aligning to the query:
6t77A Crystal structure of klebsiella pneumoniae fabg(NADPH-dependent) NADP- complex at 1.75 a resolution (see paper)
33% identity, 80% coverage: 6:245/301 of query aligns to 3:242/244 of 6t77A
- active site: G16 (= G19), S138 (= S153), Y151 (= Y166)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G15), S14 (≠ G17), R15 (≠ G18), T37 (≠ G49), L58 (≠ A70), N59 (= N71), V60 (= V75), A87 (= A102), G88 (= G103), I89 (= I104)
P0AEK2 3-oxoacyl-[acyl-carrier-protein] reductase FabG; 3-ketoacyl-acyl carrier protein reductase; Beta-Ketoacyl-acyl carrier protein reductase; Beta-ketoacyl-ACP reductase; EC 1.1.1.100 from Escherichia coli (strain K12) (see 2 papers)
33% identity, 80% coverage: 4:245/301 of query aligns to 1:242/244 of P0AEK2
- GASR 12:15 (≠ GAGG 15:18) binding
- T37 (≠ G49) binding
- N---V 59:60 (≠ NGSSV 71:75) binding
- N86 (= N101) binding
- Y151 (= Y166) mutation to F: Defect in the affinity for NADPH.
- YAAAK 151:155 (≠ YGAAK 166:170) binding
- A154 (= A169) mutation to T: Decreases in the thermolability of the reductase; when associated with K-233.
- K155 (= K170) mutation to A: Defect in the affinity for NADPH.
- I184 (≠ A198) binding
- E233 (≠ A236) mutation to K: Decreases in the thermolability of the reductase; when associated with T-154.
1q7bA The structure of betaketoacyl-[acp] reductase from e. Coli in complex with NADP+ (see paper)
33% identity, 80% coverage: 6:245/301 of query aligns to 2:241/243 of 1q7bA
- active site: G15 (= G19), E101 (≠ D117), S137 (= S153), Q147 (= Q163), Y150 (= Y166), K154 (= K170)
- binding calcium ion: E232 (≠ A236), T233 (≠ I237)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G15), S13 (≠ G17), R14 (≠ G18), T36 (≠ G49), N58 (= N71), V59 (= V75), N85 (= N101), A86 (= A102), G87 (= G103), I88 (= I104), S137 (= S153), Y150 (= Y166), K154 (= K170), P180 (= P196), G181 (vs. gap), I183 (≠ A198)
3sj7A Structure of beta-ketoacetyl-coa reductase (fabg) from staphylococcus aureus complex with NADPH (see paper)
35% identity, 79% coverage: 9:245/301 of query aligns to 2:238/239 of 3sj7A
- active site: G12 (= G19), S138 (= S153), Q148 (= Q163), Y151 (= Y166), K155 (= K170)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G15), S10 (≠ G17), R11 (≠ G18), I13 (≠ L20), N31 (= N38), Y32 (≠ S47), A33 (≠ G48), G34 (= G49), S35 (= S50), A58 (≠ S73), N59 (≠ S74), V60 (= V75), N86 (= N101), A87 (= A102), T109 (≠ V124), S138 (= S153), Y151 (= Y166), K155 (= K170), P181 (= P196), G182 (vs. gap)
1q7cA The structure of betaketoacyl-[acp] reductase y151f mutant in complex with NADPH fragment (see paper)
33% identity, 80% coverage: 6:245/301 of query aligns to 2:241/243 of 1q7cA
- active site: G15 (= G19), S137 (= S153), Q147 (= Q163), F150 (≠ Y166), K154 (= K170)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G15), S13 (≠ G17), R14 (≠ G18), A35 (≠ G48), T36 (≠ G49), L57 (≠ A70), N58 (= N71), V59 (= V75), G87 (= G103), I88 (= I104)
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
35% identity, 79% coverage: 9:245/301 of query aligns to 5:245/246 of 3osuA
7pcsB Structure of the heterotetrameric sdr family member bbscd (see paper)
35% identity, 62% coverage: 9:196/301 of query aligns to 5:182/247 of 7pcsB
- binding nicotinamide-adenine-dinucleotide: G11 (= G15), M16 (≠ L20), D35 (= D39), I36 (≠ L40), I62 (≠ V75), N88 (= N101), G90 (= G103), I138 (≠ T152), S140 (= S154), Y152 (= Y166), K156 (= K170)
Sites not aligning to the query:
Query Sequence
>CCNA_02178 CCNA_02178 short-chain alcohol dehydrogenase
MADIRFDGKVAIVTGAGGGLGRQHALELARRGAKVVVNDLGGSMDGSGGSSEAAQKVVDE
IKALGGEAIANGSSVTDDAGVALMIKQAMDTWGRIDILIANAGILRDKTLTKMELADFEL
VMQVHVFGTFKPIKAVWDIMKAQNYGRIVVTTSSSGMYGNFGQSNYGAAKMAVLGLMNTL
KLEGAKNDVKINAISPVAATRMTEGLMPPEVLAKLAPEYVTPGVVYLCSDEAPTGAILTA
GAGAFALSRIYETEGVYLGEGGLSAEEVRDSWGQITAEDGQKAYFNGGEQGQKFFRKMAG
G
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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