SitesBLAST
Comparing WP_052666539.1 NCBI__GCF_000969705.1:WP_052666539.1 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)
P96825 Putative short-chain type dehydrogenase/reductase Rv0148; EC 1.1.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
47% identity, 77% coverage: 1:244/315 of query aligns to 1:244/286 of P96825
Sites not aligning to the query:
- 280 modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
42% identity, 87% coverage: 5:278/315 of query aligns to 7:280/736 of P51659
- G16 (= G14) to S: in DBPD; no dehydrogenase activity; dbSNP:rs137853096
- R106 (= R107) 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
1zbqA Crystal structure of human 17-beta-hydroxysteroid dehydrogenase type 4 in complex with NAD
42% identity, 87% coverage: 5:278/315 of query aligns to 5:278/302 of 1zbqA
- active site: S149 (= S152), Y162 (= Y164), K166 (= K168)
- binding nicotinamide-adenine-dinucleotide: G14 (= G14), G18 (= G18), L19 (≠ I19), D38 (= D38), L39 (≠ H39), S73 (≠ T73), V74 (= V74), N97 (≠ V100), A98 (= A101), T147 (≠ F150), S149 (= S152), Y162 (= Y164), K166 (= K168), P192 (= P194), N193 (≠ I195), A194 (= A196), S196 (≠ T198), R197 (= R199), M198 (= M200)
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)
45% identity, 73% coverage: 5:234/315 of query aligns to 7:235/735 of P97852
- 16:40 (vs. 14:38, 68% identical) binding NAD(+)
1gz6A (3r)-hydroxyacyl-coa dehydrogenase fragment of rat peroxisomal multifunctional enzyme type 2 (see paper)
45% identity, 73% coverage: 5:234/315 of query aligns to 5:233/301 of 1gz6A
- active site: S149 (= S152), Y162 (= Y164), K166 (= K168)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G14), L19 (≠ I19), D38 (= D38), L39 (≠ H39), S73 (≠ T73), V74 (= V74), N97 (≠ V100), A98 (= A101), G99 (= G102), I100 (= I103), H121 (= H124), T147 (≠ F150), S149 (= S152), Y162 (= Y164), K166 (= K168), P192 (= P194), A194 (= A196), S196 (≠ T198), R197 (= R199), M198 (= M200)
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)
40% identity, 84% coverage: 8:271/315 of query aligns to 9:271/906 of P22414
Sites not aligning to the query:
- 699 binding (3R)-3-hydroxydecanoyl-CoA
- 700 binding (3R)-3-hydroxydecanoyl-CoA
- 729 binding (3R)-3-hydroxydecanoyl-CoA
- 757 binding (3R)-3-hydroxydecanoyl-CoA
- 808 binding (3R)-3-hydroxydecanoyl-CoA
- 810 binding (3R)-3-hydroxydecanoyl-CoA
- 831 binding (3R)-3-hydroxydecanoyl-CoA
- 856 binding (3R)-3-hydroxydecanoyl-CoA
- 857 binding (3R)-3-hydroxydecanoyl-CoA
- 858 binding (3R)-3-hydroxydecanoyl-CoA
O53547 Hydroxyacyl-CoA dehydrogenase ChsB1; EC 1.1.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
40% identity, 89% coverage: 5:284/315 of query aligns to 18:310/317 of O53547
- L32 (≠ I19) binding NAD(+)
- D51 (= D38) binding NAD(+)
- D82 (≠ T73) binding NAD(+)
- I83 (≠ V74) binding NAD(+)
- N108 (≠ V100) binding NAD(+)
- S168 (= S152) binding NAD(+)
- Y181 (= Y164) binding NAD(+)
- K185 (= K168) binding NAD(+)
- T215 (= T198) binding NAD(+)
7lgbA Chsb1 in complex with NAD+ (see paper)
41% identity, 85% coverage: 5:271/315 of query aligns to 3:274/282 of 7lgbA
- binding nicotinamide-adenine-dinucleotide: G12 (= G14), G16 (= G18), L17 (≠ I19), D36 (= D38), V37 (≠ H39), G64 (vs. gap), D65 (vs. gap), I66 (≠ V74), N91 (≠ V100), A92 (= A101), G93 (= G102), I94 (= I103), V114 (= V123), T149 (≠ F150), S151 (= S152), Y164 (= Y164), K168 (= K168), P194 (= P194), T198 (= T198), M200 (= M200), T201 (≠ S201)
1gz6B (3r)-hydroxyacyl-coa dehydrogenase fragment of rat peroxisomal multifunctional enzyme type 2 (see paper)
42% identity, 73% coverage: 5:234/315 of query aligns to 5:210/278 of 1gz6B
- active site: S141 (= S152), Y154 (= Y164), K158 (= K168)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G14), L19 (≠ I19), D38 (= D38), L39 (≠ H39), S65 (≠ T73), V66 (= V74), N89 (≠ V100), A90 (= A101), G91 (= G102), H113 (= H124), T139 (≠ F150), S141 (= S152), Y154 (= Y164), K158 (= K168), P184 (= P194)
3sj7A Structure of beta-ketoacetyl-coa reductase (fabg) from staphylococcus aureus complex with NADPH (see paper)
39% identity, 75% coverage: 8:242/315 of query aligns to 2:236/239 of 3sj7A
- active site: G12 (= G18), S138 (= S152), Q148 (= Q161), Y151 (= Y164), K155 (= K168)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G14), S10 (≠ G16), R11 (≠ G17), I13 (= I19), N31 (≠ A37), Y32 (≠ D38), A33 (≠ H39), G34 (= G40), S35 (= S49), A58 (≠ D72), N59 (≠ T73), V60 (= V74), N86 (≠ V100), A87 (= A101), T109 (≠ V123), S138 (= S152), Y151 (= Y164), K155 (= K168), P181 (= P194), G182 (vs. gap)
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
38% identity, 75% coverage: 8:242/315 of query aligns to 5:243/246 of 3osuA
7tzpG Crystal structure of putataive short-chain dehydrogenase/reductase (fabg) from klebsiella pneumoniae subsp. Pneumoniae ntuh-k2044 in complex with nadh (see paper)
35% identity, 76% coverage: 5:244/315 of query aligns to 6:246/247 of 7tzpG
- binding 1,4-dihydronicotinamide adenine dinucleotide: G15 (= G14), R18 (≠ G17), G19 (= G18), I20 (= I19), D39 (= D38), R40 (≠ H39), C63 (≠ D72), I65 (≠ V74), N91 (≠ V100), G93 (= G102), I94 (= I103), V114 (= V123), Y155 (= Y164), K159 (= K168), I188 (≠ A196), T190 (= T198), T193 (≠ S201)
7do6A Crystal structure of azotobacter vinelandii l-rhamnose 1- dehydrogenase(NADP bound-form) (see paper)
38% identity, 76% coverage: 4:242/315 of query aligns to 2:241/247 of 7do6A
- active site: G16 (= G18), S146 (= S152), Y159 (= Y164)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G14), S14 (≠ G16), R15 (≠ G17), G16 (= G18), I17 (= I19), H36 (≠ D38), S37 (≠ D44), G42 (≠ S49), D66 (≠ T73), A67 (≠ V74), N93 (≠ V100), A94 (= A101), G95 (= G102), I96 (= I103), T116 (≠ V123), S146 (= S152), Y159 (= Y164), K163 (= K168), I192 (= I195)
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)
39% identity, 76% coverage: 5:244/315 of query aligns to 4:245/247 of P73574
- A14 (≠ G15) mutation to G: 4.2-fold increase in activity on acetoacetyl-CoA.
- P151 (≠ I159) 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 (= K168) mutation to A: Almost no activity on acetoacetyl-CoA.
- F188 (≠ I195) mutation to Y: 3.3-fold increase in activity on acetoacetyl-CoA.
- N198 (≠ P205) mutation to R: 3.5-fold increase in activity on acetoacetyl-CoA.
7do7A Crystal structure of azotobacter vinelandii l-rhamnose 1- dehydrogenase(NAD and l-rhamnose bound-form) (see paper)
37% identity, 76% coverage: 4:242/315 of query aligns to 2:250/256 of 7do7A
- active site: G16 (= G18), S146 (= S152), Y159 (= Y164)
- binding nicotinamide-adenine-dinucleotide: G12 (= G14), R15 (≠ G17), G16 (= G18), I17 (= I19), S37 (≠ D44), D66 (≠ T73), A67 (≠ V74), N93 (≠ V100), A94 (= A101), G95 (= G102), I96 (= I103), V144 (≠ F150), S145 (≠ T151), S146 (= S152), Y159 (= Y164), K163 (= K168), P189 (= P194), G190 (vs. gap), I192 (= I195), T194 (vs. gap), I196 (vs. gap)
- binding beta-L-rhamnopyranose: F99 (≠ E106), S146 (= S152), S148 (≠ G153), Q156 (= Q161), Y159 (= Y164), N197 (vs. gap), D235 (= D227), M236 (≠ H228), R238 (≠ K230)
7b81A Crystal structure of azotobacter vinelandii l-rhamnose 1-dehydrogenase (NAD bound-form) (see paper)
37% identity, 76% coverage: 4:242/315 of query aligns to 2:250/256 of 7b81A
- active site: G16 (= G18), S146 (= S152), Y159 (= Y164)
- binding nicotinamide-adenine-dinucleotide: G12 (= G14), S14 (≠ G16), R15 (≠ G17), I17 (= I19), D66 (≠ T73), A67 (≠ V74), N93 (≠ V100), A94 (= A101), G95 (= G102), I96 (= I103), T116 (≠ V123), V144 (≠ F150), S146 (= S152), Y159 (= Y164), K163 (= K168), P189 (= P194), G190 (vs. gap), I192 (= I195), T194 (vs. gap), I196 (vs. gap)
4nbtA Crystal structure of fabg from acholeplasma laidlawii (see paper)
38% identity, 76% coverage: 5:242/315 of query aligns to 3:236/239 of 4nbtA
- active site: G16 (= G18), S132 (= S152), Y145 (= Y164), K149 (= K168)
- binding nicotinamide-adenine-dinucleotide: G12 (= G14), K15 (≠ G17), G16 (= G18), L17 (≠ I19), D36 (= D38), L37 (≠ H39), L52 (≠ D72), N53 (≠ T73), V54 (= V74), N80 (≠ V100), A81 (= A101), G82 (= G102), I130 (≠ F150), S132 (= S152), Y145 (= Y164), K149 (= K168), P177 (= P194), G178 (vs. gap), I180 (≠ A196), T182 (= T198)
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
34% identity, 76% coverage: 5:244/315 of query aligns to 3:246/247 of 4jroC
- active site: G16 (= G18), S142 (= S152), Q152 (= Q161), Y155 (= Y164), K159 (= K168)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G14), S14 (≠ G16), R15 (≠ G17), G16 (= G18), I17 (= I19), N35 (≠ A37), Y36 (≠ D38), N37 (≠ H39), G38 (= G40), S39 (= S49), N63 (≠ T73), V64 (= V74), N90 (≠ V100), A91 (= A101), I93 (= I103), I113 (≠ V123), S142 (= S152), Y155 (= Y164), K159 (= K168), P185 (= P194), I188 (≠ A196), T190 (= T198)
1edoA The x-ray structure of beta-keto acyl carrier protein reductase from brassica napus complexed with NADP+ (see paper)
35% identity, 74% coverage: 10:242/315 of query aligns to 4:241/244 of 1edoA
- active site: G12 (= G18), S138 (= S152), Y151 (= Y164), K155 (= K168)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G14), S10 (≠ G16), R11 (≠ G17), I13 (= I19), N31 (≠ G45), Y32 (≠ S46), A33 (≠ D47), R34 (≠ P48), S35 (= S49), D59 (≠ T73), V60 (= V74), N86 (≠ V100), A87 (= A101), S138 (= S152), Y151 (= Y164), K155 (= K168), P181 (= P194), G182 (vs. gap), I184 (= I195), S186 (≠ R197), M188 (≠ R199)
4i08A Crystal structure of beta-ketoacyl-acyl carrier protein reductase (fabg) from vibrio cholerae in complex with NADPH (see paper)
35% identity, 76% coverage: 5:242/315 of query aligns to 6:239/243 of 4i08A
- active site: G19 (= G18), N113 (≠ H124), S141 (≠ F150), Q151 (= Q161), Y154 (= Y164), K158 (= K168)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G14), S17 (≠ G16), R18 (≠ G17), I20 (= I19), T40 (≠ P48), N62 (≠ T73), V63 (= V74), N89 (≠ V100), A90 (= A101), G140 (= G149), S141 (≠ F150), Y154 (= Y164), K158 (= K168), P184 (= P194), G185 (vs. gap), T189 (= T198)
Query Sequence
>WP_052666539.1 NCBI__GCF_000969705.1:WP_052666539.1
MAGFLDGKAIAITGGGGGIGRAVALACAAEGAKVVVADHGVSMDGSDPSSAVADAVVEEI
RDTGGEAVAVADTVTTMEGGERVVATAVDAFGSIDGVVCVAGILRERMLFNMTEDEWDPV
VDVHLKGHFTVFRAAAARMRKARSGSLVGFTSGAFQGSIAQANYSAAKGGVVSLVRSAAV
GLAKYGVTANAIAPIARTRMSDNVPGDLAEMGDPEDVAPMVVYLLSDHAKHVTGQVYTAV
GGKIAVWNQPREVRAMHTDGRWTPEEIAARLDGTVGVEPMPIFAMLERIAASREAAAPAD
QGAAVPTATPNEGAA
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