SitesBLAST
Comparing WP_013536899.1 NCBI__GCF_000185805.1:WP_013536899.1 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)
2hk9B Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
47% identity, 95% coverage: 3:271/282 of query aligns to 2:259/267 of 2hk9B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V67 (= V68), G130 (= G131), G133 (= G134), A134 (= A135), N153 (= N155), R154 (= R156), T155 (≠ S157), K158 (= K160), T188 (= T198), S189 (= S199), V190 (≠ L200), I214 (= I224), M238 (= M250), L239 (= L251)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S20), S21 (= S22), N64 (= N65), T66 (= T67), K70 (= K71), N91 (= N92), D106 (= D107), Y216 (= Y226), L239 (= L251), Q242 (= Q254)
2hk9A Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
47% identity, 95% coverage: 3:271/282 of query aligns to 2:259/269 of 2hk9A
- binding 2'-monophosphoadenosine-5'-diphosphate: V67 (= V68), G132 (= G133), G133 (= G134), A134 (= A135), N153 (= N155), R154 (= R156), T155 (≠ S157), T188 (= T198), S189 (= S199), V190 (≠ L200)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S20), S21 (= S22), N64 (= N65), K70 (= K71), N91 (= N92), D106 (= D107), Y216 (= Y226), L239 (= L251), Q242 (= Q254)
O67049 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Aquifex aeolicus (strain VF5) (see paper)
47% identity, 95% coverage: 3:271/282 of query aligns to 2:259/269 of O67049
- SLS 19:21 (= SLS 20:22) binding shikimate
- D82 (≠ G83) binding NADP(+)
- N91 (= N92) binding shikimate
- D106 (= D107) binding shikimate
- GAGGA 130:134 (= GAGGA 131:135) binding NADP(+)
- I214 (= I224) binding NADP(+)
- Y216 (= Y226) binding shikimate
- G235 (= G247) binding NADP(+)
- Q242 (= Q254) binding shikimate
Q58484 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) (see paper)
45% identity, 97% coverage: 3:276/282 of query aligns to 2:276/282 of Q58484
1nvtB Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
45% identity, 97% coverage: 3:276/282 of query aligns to 7:281/287 of 1nvtB
- active site: K75 (= K71), D111 (= D107)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I72 (≠ V68), G135 (= G131), G137 (= G133), G138 (= G134), A139 (= A135), N157 (= N155), R158 (= R156), T159 (≠ S157), K162 (= K160), A200 (≠ T197), T201 (= T198), P202 (≠ S199), I203 (≠ L200), M205 (≠ L202), L229 (≠ I224), Y231 (= Y226), M255 (= M250), L256 (= L251)
- binding zinc ion: E22 (≠ K18), H23 (= H19)
1nvtA Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
45% identity, 97% coverage: 3:276/282 of query aligns to 7:281/287 of 1nvtA
- active site: K75 (= K71), D111 (= D107)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G135 (= G131), A139 (= A135), N157 (= N155), R158 (= R156), T159 (≠ S157), K162 (= K160), A200 (≠ T197), T201 (= T198), P202 (≠ S199), I203 (≠ L200), M205 (≠ L202), L229 (≠ I224), Y231 (= Y226), G252 (= G247), M255 (= M250), L256 (= L251)
3tnlA 1.45 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with shikimate and NAD.
37% identity, 98% coverage: 2:276/282 of query aligns to 5:287/288 of 3tnlA
- binding nicotinamide-adenine-dinucleotide: M71 (≠ V68), G134 (= G131), A135 (= A132), G136 (= G133), G137 (= G134), A138 (= A135), N158 (= N155), R159 (= R156), D161 (vs. gap), F163 (vs. gap), T207 (= T198), V209 (≠ L200), M211 (≠ L202), F214 (≠ Q205), V235 (≠ I224), Y237 (= Y226), M261 (= M250), M262 (≠ L251)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S23 (= S20), S25 (= S22), N68 (= N65), S70 (≠ T67), K74 (= K71), N95 (= N92), D110 (= D107), Q265 (= Q254)
3tozA 2.2 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with NAD.
37% identity, 98% coverage: 2:276/282 of query aligns to 8:290/291 of 3tozA
- binding nicotinamide-adenine-dinucleotide: G137 (= G131), A138 (= A132), G139 (= G133), G140 (= G134), A141 (= A135), N161 (= N155), R162 (= R156), D164 (vs. gap), F166 (vs. gap), T210 (= T198), G211 (≠ S199), V212 (≠ L200), M214 (≠ L202), F217 (≠ Q205), V238 (≠ I224), Y240 (= Y226), G261 (= G247), M264 (= M250), M265 (≠ L251)
Q8Y9N5 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
37% identity, 98% coverage: 2:276/282 of query aligns to 8:290/291 of Q8Y9N5
1npdB X-ray structure of shikimate dehydrogenase complexed with NAD+ from e.Coli (ydib) northeast structural genomics research consortium (nesg) target er24 (see paper)
36% identity, 98% coverage: 1:276/282 of query aligns to 1:284/288 of 1npdB
- binding nicotinamide-adenine-dinucleotide: A132 (= A132), G133 (= G133), G134 (= G134), A135 (= A135), N155 (= N155), R156 (= R156), D158 (vs. gap), F160 (vs. gap), T204 (= T198), K205 (≠ S199), V206 (≠ L200), M208 (≠ L202), C232 (≠ I224), M258 (= M250), L259 (= L251)
P0A6D5 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Escherichia coli (strain K12) (see 4 papers)
36% identity, 98% coverage: 1:276/282 of query aligns to 1:284/288 of P0A6D5
- M1 (= M1) modified: Initiator methionine, Removed
- S22 (= S22) mutation to A: Kinetically unchanged as compared with the wild-type.
- Y39 (= Y39) mutation to F: Kinetically unchanged as compared with the wild-type.
- S67 (≠ T67) mutation to A: Reduces activity towards quinate about 6-fold, but has a little effect on shikimate conversion.
- K71 (= K71) mutation to A: 3200-fold decrease in the affinity for quinate. 170-fold decrease in the affinity for shikimate.; mutation to G: 10-fold greater reduction in catalytic efficiency is observed with quinate than with shikimate.
- N92 (= N92) mutation to A: Alters protein structure. Loss of activity for both substrates.
- T106 (= T106) mutation to A: 2000-fold decrease in the affinity for quinate. 70-fold decrease in the affinity for shikimate. 10-fold greater reduction in catalytic efficiency is observed with quinate than with shikimate.
- D107 (= D107) mutation to A: Loss of activity towards quinate. 20000-fold decrease in the affinity for shikimate.
- AGGA 132:135 (= AGGA 132:135) binding NAD(+)
- NRRD 155:158 (≠ NRS- 155:157) binding NAD(+)
- K205 (≠ S199) binding NAD(+)
- CVYN 232:235 (≠ IIYN 224:227) binding NAD(+)
- G255 (= G247) binding NAD(+)
- Q262 (= Q254) mutation to A: 3-fold reduction in catalytic efficiency for both substrates.
1o9bA Quinate/shikimate dehydrogenase ydib complexed with nadh (see paper)
36% identity, 94% coverage: 11:276/282 of query aligns to 5:278/280 of 1o9bA
- binding 1,4-dihydronicotinamide adenine dinucleotide: A126 (= A132), G127 (= G133), G128 (= G134), A129 (= A135), R150 (= R156), F154 (vs. gap), K199 (≠ S199), V200 (≠ L200), M202 (≠ L202), C226 (≠ I224), Y228 (= Y226), M252 (= M250), L253 (= L251)
Q8ZPR4 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
38% identity, 98% coverage: 1:276/282 of query aligns to 1:284/288 of Q8ZPR4
Q5HNV1 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Staphylococcus epidermidis (strain ATCC 35984 / RP62A) (see paper)
35% identity, 96% coverage: 10:280/282 of query aligns to 3:269/269 of Q5HNV1
- SLS 13:15 (= SLS 20:22) binding shikimate
- T60 (= T67) binding shikimate
- N85 (= N92) binding shikimate
- D100 (= D107) binding shikimate
- Y211 (= Y226) Plays a major role in the catalytic process and a minor role in the substrate binding; mutation to F: Leads to a 345-fold decrease in the catalytic efficiency and a 3-fold decrease in the affinity binding for shikimate.
- Q239 (= Q254) binding shikimate
3dooA Crystal structure of shikimate dehydrogenase from staphylococcus epidermidis complexed with shikimate (see paper)
35% identity, 97% coverage: 10:282/282 of query aligns to 3:258/258 of 3dooA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S13 (= S20), S15 (= S22), N58 (= N65), T60 (= T67), K64 (= K71), N85 (= N92), D100 (= D107), F227 (≠ L251), Q230 (= Q254)
2cy0A Crystal structure of shikimate 5-dehydrogenase (aroe) from thermus thermophilus hb8 in complex with NADP (see paper)
41% identity, 90% coverage: 10:264/282 of query aligns to 4:245/262 of 2cy0A
- active site: K64 (= K71), D100 (= D107)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G123 (= G131), G126 (= G134), A127 (= A135), N146 (= N155), R147 (= R156), T148 (≠ S157), R151 (≠ K160), T179 (= T198), R180 (≠ S199), V181 (≠ L200), L205 (≠ I224), L232 (= L251)
2ev9B Crystal structure of shikimate 5-dehydrogenase (aroe) from thermus thermophilus hb8 in complex with NADP(h) and shikimate (see paper)
41% identity, 90% coverage: 10:264/282 of query aligns to 4:245/263 of 2ev9B
- active site: K64 (= K71), D100 (= D107)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S14 (= S20), S16 (= S22), N58 (= N65), T60 (= T67), K64 (= K71), N85 (= N92), D100 (= D107), Q235 (= Q254)
Q5SJF8 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
41% identity, 90% coverage: 10:264/282 of query aligns to 4:245/263 of Q5SJF8
- SLS 14:16 (= SLS 20:22) binding shikimate
- T60 (= T67) binding shikimate
- K64 (= K71) active site, Proton acceptor
- N85 (= N92) binding shikimate
- D100 (= D107) binding shikimate
- GAGGA 123:127 (= GAGGA 131:135) binding NADP(+)
- NRTPQR 146:151 (≠ NRSFPK 155:160) binding NADP(+)
- L205 (≠ I224) binding NADP(+)
- Y207 (= Y226) binding shikimate
- G228 (= G247) binding NADP(+)
- Q235 (= Q254) binding shikimate
Q9KVT3 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
35% identity, 96% coverage: 10:280/282 of query aligns to 8:278/278 of Q9KVT3
- SKS 18:20 (≠ SLS 20:22) binding shikimate
- N90 (= N92) binding shikimate
- D106 (= D107) binding shikimate
- NRTFAK 154:159 (≠ NRSFPK 155:160) binding NADP(+)
- Q248 (= Q254) binding shikimate
3pgjA 2.49 angstrom resolution crystal structure of shikimate 5- dehydrogenase (aroe) from vibrio cholerae o1 biovar eltor str. N16961 in complex with shikimate
35% identity, 95% coverage: 10:278/282 of query aligns to 4:272/272 of 3pgjA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S14 (= S20), S16 (= S22), N59 (= N65), T61 (= T67), K65 (= K71), N86 (= N92), D102 (= D107), Q244 (= Q254)
Query Sequence
>WP_013536899.1 NCBI__GCF_000185805.1:WP_013536899.1
MKLTGKTAVYGIIGHPVKHSLSPLMQTAAFEALGIDAVYVPFNLAPQNLKEGIEGLRVLG
VKGFNVTVPHKEQVAELVDFLEGDAEFLGAVNTVKNEEGQLTGYNTDAEGFLRSLLEEGV
ELEGKKALMFGAGGAARAVGYALLKGGVKFLHVVNRSFPKAKALGELLSRRGNVLVYPLR
DSVVETLLDEADIIVNTTSLGLHPQDPQLFDYSKIPEEKVVVDIIYNPPLTPLLKAAKER
GCKVINGLGMLIHQGAVAFEIWTGQKAPVKVMREVLEGELYG
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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