SitesBLAST
Comparing WP_017866878.1 NCBI__GCF_000349725.1:WP_017866878.1 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)
7m1zC Targeting enterococcus faecalis hmg-coa reductase with a novel non- statin inhibitor
45% identity, 97% coverage: 6:417/424 of query aligns to 14:422/422 of 7m1zC
- binding calcium ion: Q32 (≠ K24), I33 (≠ L25), P88 (= P80), D159 (≠ A154), L160 (= L155), L380 (= L375), R383 (≠ K378)
- binding (r)-mevalonate: E87 (= E79), R258 (= R253), T261 (= T256), N268 (= N263)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: E87 (= E79), S149 (= S144), R153 (= R148), V178 (≠ T173), K179 (= K174), A181 (= A176), M182 (= M177), G183 (= G178), A184 (= A179), N185 (= N180), N214 (= N208), K264 (= K259), V324 (= V319), G326 (= G321), H377 (= H372), N410 (≠ Q403), Q411 (= Q404)
7m3hA Targeting enterococcus faecalis hmg-coa reductase with a novel non- statin inhibitor
45% identity, 97% coverage: 6:417/424 of query aligns to 1:409/409 of 7m3hA
7m1zB Targeting enterococcus faecalis hmg-coa reductase with a novel non- statin inhibitor
45% identity, 97% coverage: 6:417/424 of query aligns to 17:425/425 of 7m1zB
- binding calcium ion: D162 (≠ A154), L163 (= L155)
- binding 3-hydroxy-3-methylglutaryl-coenzyme a: H74 (≠ N63), E90 (= E79), S92 (= S81), A95 (= A84), A96 (≠ G85), N99 (≠ H88), K102 (≠ A91), K237 (= K228), R261 (= R253), T264 (= T256), A367 (= A359), I376 (= I368), L383 (= L375)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: Y150 (≠ H142), S152 (= S144), R156 (= R148), V181 (≠ T173), D183 (≠ E175), A184 (= A176), A187 (= A179), N188 (= N180), L215 (= L206), N217 (= N208), V327 (= V319)
5wpkB Structure of the class ii 3-hydroxy-3-methylglutaryl-coa reductase from streptococcus pneumoniae bound to hmg-coa and in a partially closed conformation (see paper)
47% identity, 98% coverage: 3:418/424 of query aligns to 5:422/422 of 5wpkB
- binding 3-hydroxy-3-methylglutaryl-coenzyme a: S7 (≠ E5), E48 (= E48), N49 (= N49), E79 (= E79), A84 (= A84), A85 (≠ G85), Y88 (≠ H88), R255 (= R253), T258 (= T256), A363 (= A359), L367 (= L363), I372 (= I368), K378 (≠ N374), L379 (= L375)
5wpjA Structure of the class ii 3-hydroxy-3-methylglutaryl-coa reductase from streptococcus pneumoniae bound to NADPH in open conformations (see paper)
48% identity, 86% coverage: 3:365/424 of query aligns to 5:369/369 of 5wpjA
6dioC Structure of class ii hmg-coa reductase from delftia acidovorans with NAD bound (see paper)
40% identity, 92% coverage: 4:394/424 of query aligns to 6:402/428 of 6dioC
Sites not aligning to the query:
1qaxA Ternary complex of pseudomonas mevalonii hmg-coa reductase with hmg- coa and NAD+ (see paper)
40% identity, 90% coverage: 15:394/424 of query aligns to 15:400/425 of 1qaxA
- binding 3-hydroxy-3-methylglutaryl-coenzyme a: E80 (= E79), A85 (= A84), Y89 (≠ H88), K92 (≠ A91), R258 (= R253), T261 (= T256), G265 (= G260), N268 (= N263), Q361 (= Q355), A365 (= A359), L369 (= L363)
- binding nicotinamide-adenine-dinucleotide: E80 (= E79), K264 (= K259)
Sites not aligning to the query:
P13702 3-hydroxy-3-methylglutaryl-coenzyme A reductase; HMG-CoA reductase; EC 1.1.1.88 from Pseudomonas mevalonii (see 2 papers)
40% identity, 90% coverage: 15:394/424 of query aligns to 18:403/428 of P13702
- E52 (= E48) mutation to Q: No loss of activity.
- E83 (= E79) mutation to Q: Greatly reduced activity.
- D183 (≠ E175) mutation D->A,N: Reduced activity.
- H381 (= H372) active site, Proton donor; mutation H->A,N,Q,K: Reduced activity.
8vlqA 3-hydroxy-3-methylglutaryl-coenzyme A reductase (see paper)
40% identity, 90% coverage: 13:394/424 of query aligns to 15:402/421 of 8vlqA
- binding (R)-mevaldehyde: E82 (= E79), R260 (= R253), T263 (= T256), K266 (= K259), N270 (= N263), A367 (= A359)
- binding coenzyme a: E82 (= E79), S84 (= S81), A87 (= A84), A88 (≠ G85), Y91 (≠ H88), A367 (= A359), R378 (≠ K370), G379 (= G371), H380 (= H372)
- binding nicotinamide-adenine-dinucleotide: E82 (= E79), K266 (= K259), H384 (≠ Q376), V391 (≠ S383)
- binding 1,4-dihydronicotinamide adenine dinucleotide: E82 (= E79), K266 (= K259), H384 (≠ Q376), V391 (≠ S383)
- binding Mevaldyl-Coenzyme A: E82 (= E79), S84 (= S81), A87 (= A84), A88 (≠ G85), Y91 (≠ H88), R260 (= R253), T263 (= T256), N270 (= N263), A367 (= A359), I376 (= I368), R378 (≠ K370), G379 (= G371)
Sites not aligning to the query:
8gdnA Structure of pmhmgr bound to mevalonate, coa and NAD. (see paper)
40% identity, 90% coverage: 13:394/424 of query aligns to 15:402/421 of 8gdnA
- binding coenzyme a: S84 (= S81), A87 (= A84), A88 (≠ G85), Y91 (≠ H88), K94 (≠ A91), A367 (= A359), H380 (= H372)
- binding (r)-mevalonate: E82 (= E79), R260 (= R253), T263 (= T256), K266 (= K259), N270 (= N263), A367 (= A359)
- binding nicotinamide-adenine-dinucleotide: E82 (= E79), K266 (= K259), H384 (≠ Q376), I388 (≠ L380), V391 (≠ S383)
- binding sulfate ion: R97 (≠ K94)
Sites not aligning to the query:
4i4bA Hmg-coa reductase from pseudomonas mevalonii complexed with NAD and intermediate hemiacetal form of hmg-coa (see paper)
40% identity, 89% coverage: 13:388/424 of query aligns to 14:395/410 of 4i4bA
- binding (3R,5R,9R,19R,21S)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9,21-tetrahydroxy-8,8,21-trimethyl-10,14-dioxo-19-sulfanyl-2,4,6-trioxa-18-thia-11,15-diaza-3,5-diphosphatricosan-23-oic acid 3,5-dioxide: E81 (= E79), S83 (= S81), A86 (= A84), A87 (≠ G85), Y90 (≠ H88), K93 (≠ A91), R259 (= R253), T262 (= T256), A366 (= A359), I375 (= I368)
- binding nicotinamide-adenine-dinucleotide: E81 (= E79), K265 (= K259), H383 (≠ Q376), I387 (≠ L380), V390 (≠ S383)
Sites not aligning to the query:
- binding (3R,5R,9R,19R,21S)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9,21-tetrahydroxy-8,8,21-trimethyl-10,14-dioxo-19-sulfanyl-2,4,6-trioxa-18-thia-11,15-diaza-3,5-diphosphatricosan-23-oic acid 3,5-dioxide: 9
1qayA Ternary complex of pseudomonas mevalonii hmg-coa reductase with mevalonate and NAD+ (see paper)
40% identity, 86% coverage: 15:378/424 of query aligns to 15:384/384 of 1qayA
6eevA Structure of class ii hmg-coa reductase from delftia acidovorans with mevalonate bound (see paper)
39% identity, 86% coverage: 4:367/424 of query aligns to 5:374/374 of 6eevA
4i6yB 3-hydroxy-3-methyl (hmg) coenzyme a reductase bound to r-mevalonate (see paper)
40% identity, 84% coverage: 15:370/424 of query aligns to 16:377/377 of 4i6yB
8sz6B Pmhmgr bound to mevaldehyde and coa (see paper)
40% identity, 84% coverage: 15:369/424 of query aligns to 17:377/377 of 8sz6B
Sites not aligning to the query:
8sz6A Pmhmgr bound to mevaldehyde and coa (see paper)
40% identity, 84% coverage: 15:369/424 of query aligns to 17:377/377 of 8sz6A
Sites not aligning to the query:
4i4bB Hmg-coa reductase from pseudomonas mevalonii complexed with NAD and intermediate hemiacetal form of hmg-coa (see paper)
40% identity, 84% coverage: 15:369/424 of query aligns to 16:376/376 of 4i4bB
- binding (3S)-3-hydroxy-3-methyl-5-sulfanylpentanoic acid: E81 (= E79), R259 (= R253), T262 (= T256), K265 (= K259), N269 (= N263)
- binding (3R,5R,9R,19R,21S)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9,21-tetrahydroxy-8,8,21-trimethyl-10,14-dioxo-19-sulfanyl-2,4,6-trioxa-18-thia-11,15-diaza-3,5-diphosphatricosan-23-oic acid 3,5-dioxide: E50 (= E48), N51 (= N49)
- binding nicotinamide-adenine-dinucleotide: D144 (≠ H142), L146 (≠ S144), L150 (≠ R148), R180 (≠ K174), D181 (≠ E175), A182 (= A176), M183 (= M177), G184 (= G178), A185 (= A179), N186 (= N180), T187 (≠ M181), L212 (= L206), N214 (= N208), D281 (= D275), G327 (= G320), G328 (= G321)
1r31A Hmg-coa reductase from pseudomonas mevalonii complexed with hmg-coa
40% identity, 84% coverage: 15:369/424 of query aligns to 16:376/376 of 1r31A
Sites not aligning to the query:
4i56A Hmg-coa reductase from pseudomonas mevalonii complexed with dithio- hmg-coa (see paper)
39% identity, 83% coverage: 13:366/424 of query aligns to 14:373/373 of 4i56A
- binding (3S,5S,9R,21S)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9,21-tetrahydroxy-8,8,21-trimethyl-10,14-dioxo-19-thioxo-2,4,6-trioxa-18-thia-11,15-diaza-3,5-diphosphatricosan-23-oic acid 3,5-dioxide: S83 (= S81), A86 (= A84), A87 (≠ G85), Y90 (≠ H88), K93 (≠ A91), R259 (= R253), T262 (= T256), G266 (= G260), N269 (= N263), G365 (≠ A358), A366 (= A359), A369 (= A362)
Sites not aligning to the query:
- binding (3S,5S,9R,21S)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9,21-tetrahydroxy-8,8,21-trimethyl-10,14-dioxo-19-thioxo-2,4,6-trioxa-18-thia-11,15-diaza-3,5-diphosphatricosan-23-oic acid 3,5-dioxide: 9
1t02A Crystal structure of a statin bound to class ii hmg-coa reductase (see paper)
39% identity, 83% coverage: 13:365/424 of query aligns to 13:371/371 of 1t02A
- binding (3r,5r)-7-((1r,2r,6s,8r,8as)-2,6-dimethyl-8-{[(2r)-2-methylbutanoyl]oxy}-1,2,6,7,8,8a-hexahydronaphthalen-1-yl)-3,5-dihydroxyheptanoic acid: E80 (= E79), S82 (= S81), A86 (≠ G85), R258 (= R253), T261 (= T256), K264 (= K259), N268 (= N263), Q361 (= Q355), A365 (= A359)
Query Sequence
>WP_017866878.1 NCBI__GCF_000349725.1:WP_017866878.1
MQGFEKYYRKTWSQRLDILTQQNKLSEKQVEQLKQNAVTPVLGEAQIENFLTQFQLPEGL
ALNFVIDGKEYLIPMVIEEPSVIAGASHGAAIVKKTGGFHTKSSRRAMRGQVVLENVTDL
VATKKKIEEQETELMQAAVDAHPSIVKRGGGPLALKVRILEQGLLSVDLIIDTKEAMGAN
MINSMLEAVADKLRTTGHHDVLMAILSNYTTECLVTASCQIPVANLAKNGLPGLKIAQKL
AQASRVAQVDPYRAATHNKGIMNGIDAAVIASGNDWRAIEAAAHAYAARDGQYRGLSTWK
VAGDQLEGELSLPVPVGSVGGSIGIVPLVQVNSALRSEKDALGLEKIIASVGLAQNLAAL
YALVTDGIQKGHMNLQMKSLAVSVGAKEDEIEQVVSVLQKLPQQDQAIAQHVLDEIRNEA
SENE
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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