SitesBLAST
Comparing WP_013420275.1 NCBI__GCF_000166055.1:WP_013420275.1 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)
2hk9A Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
38% identity, 90% coverage: 6:256/278 of query aligns to 11:254/269 of 2hk9A
- binding 2'-monophosphoadenosine-5'-diphosphate: V67 (= V62), G132 (= G128), G133 (= G129), A134 (= A130), N153 (= N150), R154 (= R151), T155 (= T152), T188 (≠ S188), S189 (≠ T189), V190 (≠ L190)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S14), S21 (= S16), N64 (= N59), K70 (= K65), N91 (= N86), D106 (= D101), Y216 (= Y216), L239 (= L241), Q242 (= Q244)
2hk9B Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
38% identity, 90% coverage: 6:256/278 of query aligns to 11:254/267 of 2hk9B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V67 (= V62), G130 (= G126), G133 (= G129), A134 (= A130), N153 (= N150), R154 (= R151), T155 (= T152), K158 (≠ T155), T188 (≠ S188), S189 (≠ T189), V190 (≠ L190), I214 (= I214), M238 (= M240), L239 (= L241)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S14), S21 (= S16), N64 (= N59), T66 (= T61), K70 (= K65), N91 (= N86), D106 (= D101), Y216 (= Y216), L239 (= L241), Q242 (= Q244)
O67049 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Aquifex aeolicus (strain VF5) (see paper)
39% identity, 90% coverage: 6:254/278 of query aligns to 11:252/269 of O67049
- SLS 19:21 (= SLS 14:16) binding shikimate
- D82 (≠ A77) binding NADP(+)
- N91 (= N86) binding shikimate
- D106 (= D101) binding shikimate
- GAGGA 130:134 (= GAGGA 126:130) binding NADP(+)
- I214 (= I214) binding NADP(+)
- Y216 (= Y216) binding shikimate
- G235 (= G237) binding NADP(+)
- Q242 (= Q244) 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)
35% identity, 96% coverage: 6:272/278 of query aligns to 11:281/282 of Q58484
1nvtB Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
35% identity, 97% coverage: 2:272/278 of query aligns to 12:286/287 of 1nvtB
- active site: K75 (= K65), D111 (= D101)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I72 (≠ V62), G135 (= G126), G137 (= G128), G138 (= G129), A139 (= A130), N157 (= N150), R158 (= R151), T159 (= T152), K162 (≠ T155), A200 (≠ T187), T201 (≠ S188), P202 (≠ T189), I203 (≠ L190), M205 (= M192), L229 (≠ I214), Y231 (= Y216), M255 (= M240), L256 (= L241)
- binding zinc ion: E22 (≠ S12), H23 (= H13)
1nvtA Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
35% identity, 97% coverage: 2:272/278 of query aligns to 12:286/287 of 1nvtA
- active site: K75 (= K65), D111 (= D101)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G135 (= G126), A139 (= A130), N157 (= N150), R158 (= R151), T159 (= T152), K162 (≠ T155), A200 (≠ T187), T201 (≠ S188), P202 (≠ T189), I203 (≠ L190), M205 (= M192), L229 (≠ I214), Y231 (= Y216), G252 (= G237), M255 (= M240), L256 (= L241)
Q5HNV1 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Staphylococcus epidermidis (strain ATCC 35984 / RP62A) (see paper)
32% identity, 92% coverage: 3:259/278 of query aligns to 2:254/269 of Q5HNV1
- SLS 13:15 (= SLS 14:16) binding shikimate
- T60 (= T61) binding shikimate
- N85 (= N86) binding shikimate
- D100 (= D101) binding shikimate
- Y211 (= Y216) 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 (= Q244) binding shikimate
Q9KVT3 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
37% identity, 93% coverage: 6:264/278 of query aligns to 10:271/278 of Q9KVT3
- SKS 18:20 (≠ SLS 14:16) binding shikimate
- N90 (= N86) binding shikimate
- D106 (= D101) binding shikimate
- NRTFAK 154:159 (≠ NRTKAT 150:155) binding NADP(+)
- Q248 (= Q244) 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
37% identity, 93% coverage: 6:264/278 of query aligns to 6:267/272 of 3pgjA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S14 (= S14), S16 (= S16), N59 (= N59), T61 (= T61), K65 (= K65), N86 (= N86), D102 (= D101), Q244 (= Q244)
P15770 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Escherichia coli (strain K12) (see paper)
38% identity, 95% coverage: 1:264/278 of query aligns to 1:264/272 of P15770
1nytA Shikimate dehydrogenase aroe complexed with NADP+ (see paper)
38% identity, 95% coverage: 1:264/278 of query aligns to 1:264/271 of 1nytA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K65 (= K65), D102 (= D101), G128 (= G128), G129 (= G129), A130 (= A130), N149 (= N150), R150 (= R151), T151 (= T152), R154 (≠ T155), T188 (≠ S188), S189 (≠ T189), S190 (≠ L190), M213 (≠ I214), G237 (= G237), M240 (= M240), L241 (= L241)
3dooA Crystal structure of shikimate dehydrogenase from staphylococcus epidermidis complexed with shikimate (see paper)
31% identity, 92% coverage: 3:259/278 of query aligns to 2:245/258 of 3dooA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S13 (= S14), S15 (= S16), N58 (= N59), T60 (= T61), K64 (= K65), N85 (= N86), D100 (= D101), F227 (≠ L241), Q230 (= Q244)
3sefA 2.4 angstrom resolution crystal structure of shikimate 5-dehydrogenase (aroe) from vibrio cholerae o1 biovar eltor str. N16961 in complex with shikimate and NADPH
37% identity, 93% coverage: 6:264/278 of query aligns to 6:263/268 of 3sefA
3sefC 2.4 angstrom resolution crystal structure of shikimate 5-dehydrogenase (aroe) from vibrio cholerae o1 biovar eltor str. N16961 in complex with shikimate and NADPH
35% identity, 93% coverage: 6:264/278 of query aligns to 6:240/244 of 3sefC
3tozA 2.2 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with NAD.
35% identity, 89% coverage: 6:252/278 of query aligns to 18:276/291 of 3tozA
- binding nicotinamide-adenine-dinucleotide: G137 (= G126), A138 (= A127), G139 (= G128), G140 (= G129), A141 (= A130), N161 (= N150), R162 (= R151), D164 (≠ K153), F166 (vs. gap), T210 (≠ S188), G211 (≠ T189), V212 (≠ L190), M214 (= M192), F217 (vs. gap), V238 (≠ I214), Y240 (= Y216), G261 (= G237), M264 (= M240), M265 (≠ L241)
Q8Y9N5 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
35% identity, 89% coverage: 6:252/278 of query aligns to 18:276/291 of Q8Y9N5
3tnlA 1.45 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with shikimate and NAD.
35% identity, 89% coverage: 6:252/278 of query aligns to 15:273/288 of 3tnlA
- binding nicotinamide-adenine-dinucleotide: M71 (≠ V62), G134 (= G126), A135 (= A127), G136 (= G128), G137 (= G129), A138 (= A130), N158 (= N150), R159 (= R151), D161 (≠ K153), F163 (vs. gap), T207 (≠ S188), V209 (≠ L190), M211 (= M192), F214 (vs. gap), V235 (≠ I214), Y237 (= Y216), M261 (= M240), M262 (≠ L241)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S23 (= S14), S25 (= S16), N68 (= N59), S70 (≠ T61), K74 (= K65), N95 (= N86), D110 (= D101), Q265 (= Q244)
1o9bA Quinate/shikimate dehydrogenase ydib complexed with nadh (see paper)
34% identity, 90% coverage: 6:254/278 of query aligns to 6:266/280 of 1o9bA
- binding 1,4-dihydronicotinamide adenine dinucleotide: A126 (= A127), G127 (= G128), G128 (= G129), A129 (= A130), R150 (= R151), F154 (vs. gap), K199 (≠ T189), V200 (≠ L190), M202 (= M192), C226 (≠ I214), Y228 (= Y216), M252 (= M240), L253 (= L241)
1npdB X-ray structure of shikimate dehydrogenase complexed with NAD+ from e.Coli (ydib) northeast structural genomics research consortium (nesg) target er24 (see paper)
34% identity, 90% coverage: 6:254/278 of query aligns to 12:272/288 of 1npdB
- binding nicotinamide-adenine-dinucleotide: A132 (= A127), G133 (= G128), G134 (= G129), A135 (= A130), N155 (= N150), R156 (= R151), D158 (vs. gap), F160 (vs. gap), T204 (≠ S188), K205 (≠ T189), V206 (≠ L190), M208 (= M192), C232 (≠ I214), M258 (= M240), L259 (= L241)
P0A6D5 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Escherichia coli (strain K12) (see 4 papers)
34% identity, 90% coverage: 6:254/278 of query aligns to 12:272/288 of P0A6D5
- S22 (= S16) mutation to A: Kinetically unchanged as compared with the wild-type.
- Y39 (= Y33) mutation to F: Kinetically unchanged as compared with the wild-type.
- S67 (≠ T61) mutation to A: Reduces activity towards quinate about 6-fold, but has a little effect on shikimate conversion.
- K71 (= K65) 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 (= N86) mutation to A: Alters protein structure. Loss of activity for both substrates.
- T106 (= T100) 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 (= D101) mutation to A: Loss of activity towards quinate. 20000-fold decrease in the affinity for shikimate.
- AGGA 132:135 (= AGGA 127:130) binding NAD(+)
- NRRD 155:158 (≠ NR-- 150:151) binding NAD(+)
- K205 (≠ T189) binding NAD(+)
- CVYN 232:235 (≠ IVYT 214:217) binding NAD(+)
- G255 (= G237) binding NAD(+)
- Q262 (= Q244) mutation to A: 3-fold reduction in catalytic efficiency for both substrates.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
Query Sequence
>WP_013420275.1 NCBI__GCF_000166055.1:WP_013420275.1
MKRACVIGWPISHSLSPVIHGFWLREHGIAGEYGKAAVEPKDFADFVRGFAAAGLAGGNV
TVPHKLEAFRLADMRDAAAEAIGAVNTLWLDGGKLHGANTDAFGFLANLDEQAPDWDKSG
AAVVIGAGGAARAIVWALIERGFAEIRIVNRTKATADALAAEFPPATSFALNDLPAALDG
AHFIVNTSTLGMKGQPPLDIDLSPVAANATVNDIVYTPLETPLLAQARARGLHAVDGLGM
LLHQAAPGFELWFGVRPRVTPELRAAVLDAIAAREASA
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