SitesBLAST
Comparing N515DRAFT_3412 FitnessBrowser__Dyella79:N515DRAFT_3412 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)
P44774 Shikimate dehydrogenase-like protein HI_0607; SDH-L; EC 1.1.1.25 from Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) (see paper)
63% identity, 98% coverage: 5:269/271 of query aligns to 2:267/271 of P44774
- K67 (= K70) mutation K->A,H,N: Loss of activity.
- D103 (= D106) mutation D->A,N: Loss of activity.
1npdB X-ray structure of shikimate dehydrogenase complexed with NAD+ from e.Coli (ydib) northeast structural genomics research consortium (nesg) target er24 (see paper)
33% identity, 85% coverage: 25:254/271 of query aligns to 24:272/288 of 1npdB
- binding nicotinamide-adenine-dinucleotide: A132 (≠ S130), G133 (= G131), G134 (= G132), A135 (≠ M133), N155 (≠ A153), R156 (vs. gap), D158 (≠ N155), F160 (≠ T157), T204 (= T186), K205 (≠ P187), V206 (≠ L188), M208 (= M190), C232 (≠ V214), M258 (≠ V240), L259 (≠ I241)
P0A6D5 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Escherichia coli (strain K12) (see 4 papers)
33% identity, 85% coverage: 25:254/271 of query aligns to 24:272/288 of P0A6D5
- Y39 (= Y40) mutation to F: Kinetically unchanged as compared with the wild-type.
- S67 (= S66) mutation to A: Reduces activity towards quinate about 6-fold, but has a little effect on shikimate conversion.
- K71 (= K70) 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 (= N91) mutation to A: Alters protein structure. Loss of activity for both substrates.
- T106 (= T105) 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 (= D106) mutation to A: Loss of activity towards quinate. 20000-fold decrease in the affinity for shikimate.
- AGGA 132:135 (≠ SGGM 130:133) binding
- NRRD 155:158 (≠ A-RN 153:155) binding
- K205 (≠ P187) binding
- CVYN 232:235 (≠ VVAL 214:217) binding
- G255 (= G237) binding
- 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
- 22 S→A: Kinetically unchanged as compared with the wild-type.
1o9bA Quinate/shikimate dehydrogenase ydib complexed with nadh (see paper)
33% identity, 85% coverage: 25:254/271 of query aligns to 18:266/280 of 1o9bA
- binding 1,4-dihydronicotinamide adenine dinucleotide: A126 (≠ S130), G127 (= G131), G128 (= G132), A129 (≠ M133), R150 (vs. gap), F154 (≠ T157), K199 (≠ P187), V200 (≠ L188), M202 (= M190), C226 (≠ V214), Y228 (≠ A216), M252 (≠ V240), L253 (≠ I241)
2hk9B Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
29% identity, 85% coverage: 26:254/271 of query aligns to 24:252/267 of 2hk9B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V67 (≠ M67), G130 (= G129), G133 (= G132), A134 (≠ M133), N153 (= N155), R154 (≠ E156), T155 (= T157), K158 (≠ R160), T188 (= T186), S189 (≠ P187), V190 (≠ L188), I214 (≠ V214), M238 (≠ V240), L239 (≠ I241)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: N64 (≠ A64), T66 (≠ S66), K70 (= K70), N91 (= N91), D106 (= D106), Y216 (≠ A216), L239 (≠ I241), Q242 (= Q244)
Sites not aligning to the query:
2hk9A Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
29% identity, 85% coverage: 26:254/271 of query aligns to 24:252/269 of 2hk9A
- binding 2'-monophosphoadenosine-5'-diphosphate: V67 (≠ M67), G132 (= G131), G133 (= G132), A134 (≠ M133), N153 (= N155), R154 (≠ E156), T155 (= T157), T188 (= T186), S189 (≠ P187), V190 (≠ L188)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: N64 (≠ A64), K70 (= K70), N91 (= N91), D106 (= D106), Y216 (≠ A216), L239 (≠ I241), Q242 (= Q244)
Sites not aligning to the query:
O67049 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Aquifex aeolicus (strain VF5) (see paper)
29% identity, 85% coverage: 26:254/271 of query aligns to 24:252/269 of O67049
Sites not aligning to the query:
3tnlA 1.45 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with shikimate and NAD.
28% identity, 93% coverage: 1:253/271 of query aligns to 2:274/288 of 3tnlA
- binding nicotinamide-adenine-dinucleotide: M71 (= M67), G134 (= G129), A135 (≠ S130), G136 (= G131), G137 (= G132), A138 (≠ M133), N158 (≠ A153), R159 (= R154), D161 (≠ E156), F163 (vs. gap), T207 (= T186), V209 (≠ L188), M211 (= M190), F214 (≠ P193), V235 (= V214), Y237 (≠ A216), M261 (≠ V240), M262 (≠ I241)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S23 (≠ N21), S25 (≠ G23), N68 (≠ A64), S70 (= S66), K74 (= K70), N95 (= N91), D110 (= D106), Q265 (= Q244)
3tozA 2.2 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with NAD.
28% identity, 93% coverage: 1:253/271 of query aligns to 5:277/291 of 3tozA
- binding nicotinamide-adenine-dinucleotide: G137 (= G129), A138 (≠ S130), G139 (= G131), G140 (= G132), A141 (≠ M133), N161 (≠ A153), R162 (= R154), D164 (≠ E156), F166 (vs. gap), T210 (= T186), G211 (≠ P187), V212 (≠ L188), M214 (= M190), F217 (≠ P193), V238 (= V214), Y240 (≠ A216), G261 (= G237), M264 (≠ V240), M265 (≠ I241)
Q8Y9N5 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
28% identity, 93% coverage: 1:253/271 of query aligns to 5:277/291 of Q8Y9N5
Q8ZPR4 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
30% identity, 85% coverage: 25:254/271 of query aligns to 24:272/288 of Q8ZPR4
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)
30% identity, 91% coverage: 12:257/271 of query aligns to 8:267/282 of Q58484
1nvtB Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
30% identity, 91% coverage: 12:257/271 of query aligns to 13:272/287 of 1nvtB
- active site: K75 (= K70), D111 (= D106)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I72 (≠ M67), G135 (≠ R128), G137 (≠ S130), G138 (= G131), A139 (≠ G132), N157 (= N155), R158 (≠ E156), T159 (= T157), K162 (≠ R160), A200 (≠ V185), T201 (= T186), P202 (= P187), I203 (≠ L188), M205 (= M190), L229 (≠ V214), Y231 (≠ A216), M255 (≠ V240), L256 (≠ I241)
- binding zinc ion: E22 (vs. gap), H23 (≠ G20)
1nvtA Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
30% identity, 91% coverage: 12:257/271 of query aligns to 13:272/287 of 1nvtA
- active site: K75 (= K70), D111 (= D106)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G135 (≠ R128), A139 (≠ G132), N157 (= N155), R158 (≠ E156), T159 (= T157), K162 (≠ R160), A200 (≠ V185), T201 (= T186), P202 (= P187), I203 (≠ L188), M205 (= M190), L229 (≠ V214), Y231 (≠ A216), G252 (= G237), M255 (≠ V240), L256 (≠ I241)
2cy0A Crystal structure of shikimate 5-dehydrogenase (aroe) from thermus thermophilus hb8 in complex with NADP (see paper)
33% identity, 89% coverage: 29:270/271 of query aligns to 22:261/262 of 2cy0A
- active site: K64 (= K70), D100 (= D106)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G123 (= G129), G126 (= G132), A127 (≠ M133), N146 (= N155), R147 (≠ E156), T148 (= T157), R151 (= R160), T179 (= T186), R180 (≠ P187), V181 (≠ L188), L205 (≠ V214), L232 (≠ I241)
2ev9B Crystal structure of shikimate 5-dehydrogenase (aroe) from thermus thermophilus hb8 in complex with NADP(h) and shikimate (see paper)
33% identity, 89% coverage: 29:270/271 of query aligns to 22:261/263 of 2ev9B
- active site: K64 (= K70), D100 (= D106)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: N58 (≠ A64), T60 (≠ S66), K64 (= K70), N85 (= N91), D100 (= D106), Q235 (= Q244)
Sites not aligning to the query:
Q5SJF8 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
33% identity, 89% coverage: 29:270/271 of query aligns to 22:261/263 of Q5SJF8
Sites not aligning to the query:
Q9X5C9 Quinate/shikimate dehydrogenase (NAD(+)); QSDH; EC 1.1.1.-; EC 1.1.1.24 from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see paper)
31% identity, 79% coverage: 46:258/271 of query aligns to 49:272/283 of Q9X5C9
- T69 (≠ S66) binding ; binding
- K73 (= K70) active site, Proton acceptor; binding ; binding
- N94 (= N91) binding ; binding
- D110 (= D106) binding ; binding
- GV 137:138 (≠ GM 132:133) binding
- D158 (≠ A153) binding
- R163 (≠ T158) binding
- PMGM 203:206 (≠ PLGM 187:190) binding
- A213 (= A199) binding
- V228 (= V214) binding
- G251 (= G237) binding
- Q258 (= Q244) binding ; binding
Sites not aligning to the query:
3jyqA Quinate dehydrogenase from corynebacterium glutamicum in complex with shikimate and nadh (see paper)
31% identity, 79% coverage: 46:258/271 of query aligns to 48:271/282 of 3jyqA
- binding nicotinamide-adenine-dinucleotide: V132 (≠ R128), G135 (= G131), G136 (= G132), V137 (≠ M133), D157 (≠ A153), L158 (≠ R154), R162 (≠ T158), T201 (= T186), P202 (= P187), M205 (= M190), V227 (= V214), A254 (≠ I241)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: N66 (≠ A64), T68 (≠ S66), N93 (= N91), D109 (= D106), Q257 (= Q244)
Sites not aligning to the query:
3jypA Quinate dehydrogenase from corynebacterium glutamicum in complex with quinate and nadh (see paper)
31% identity, 79% coverage: 46:258/271 of query aligns to 48:271/282 of 3jypA
- binding nicotinamide-adenine-dinucleotide: V132 (≠ R128), G135 (= G131), V137 (≠ M133), D157 (≠ A153), L158 (≠ R154), R162 (≠ T158), T201 (= T186), P202 (= P187), M205 (= M190), A212 (= A199), V227 (= V214), Y229 (≠ A216), A254 (≠ I241)
- binding (1S,3R,4S,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid: N66 (≠ A64), T68 (≠ S66), K72 (= K70), N93 (= N91), D109 (= D106), Q257 (= Q244)
Sites not aligning to the query:
Query Sequence
>N515DRAFT_3412 FitnessBrowser__Dyella79:N515DRAFT_3412
MTLRISRDTQLCMSLSGRPGNFGTRFQNYLYEALGLDYVYKAFTTRDLPAAIGGIRALGI
RGCAVSMPFKEACMPLVDSIDASAQAIESVNTIVNDDGHLRAYNTDYIAVARLIEQHRVA
PETTLALRGSGGMAKAVACALRDKGFRRGHIIARNETTGRALAQTCGYAWAPDMRDVEAQ
LLINVTPLGMEGPEAESLAFTEAEVERASVVFDVVALPPETPLIRLARARGKQVITGAEV
IVLQAVEQFVLYTGVRPEDALIAEAAAHALS
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