SitesBLAST
Comparing PfGW456L13_2490 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_2490 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)
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)
56% identity, 98% coverage: 6:272/272 of query aligns to 3:269/271 of P44774
- K67 (= K70) mutation K->A,H,N: Loss of activity.
- D103 (= D106) mutation D->A,N: Loss of activity.
2hk9A Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
32% identity, 92% coverage: 6:255/272 of query aligns to 3:252/269 of 2hk9A
- binding 2'-monophosphoadenosine-5'-diphosphate: V67 (≠ M67), G132 (= G131), G133 (= G132), A134 (≠ M133), N153 (≠ V152), R154 (≠ A153), T155 (≠ R154), T188 (= T186), S189 (≠ P187), V190 (≠ I188)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (≠ G23), S21 (≠ R25), N64 (≠ G64), K70 (= K70), N91 (= N91), D106 (= D106), Y216 (≠ P219), L239 (≠ I242), Q242 (= Q245)
2hk9B Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
32% identity, 92% coverage: 6:255/272 of query aligns to 3:252/267 of 2hk9B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V67 (≠ M67), G130 (= G129), G133 (= G132), A134 (≠ M133), N153 (≠ V152), R154 (≠ A153), T155 (≠ R154), K158 (≠ R157), T188 (= T186), S189 (≠ P187), V190 (≠ I188), I214 (≠ V215), M238 (≠ V241), L239 (≠ I242)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (≠ G23), S21 (≠ R25), N64 (≠ G64), T66 (≠ S66), K70 (= K70), N91 (= N91), D106 (= D106), Y216 (≠ P219), L239 (≠ I242), Q242 (= Q245)
O67049 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Aquifex aeolicus (strain VF5) (see paper)
32% identity, 92% coverage: 6:255/272 of query aligns to 3:252/269 of O67049
1o9bA Quinate/shikimate dehydrogenase ydib complexed with nadh (see paper)
31% identity, 90% coverage: 25:269/272 of query aligns to 18:280/280 of 1o9bA
- binding 1,4-dihydronicotinamide adenine dinucleotide: A126 (≠ S130), G127 (= G131), G128 (= G132), A129 (≠ M133), R150 (≠ A153), F154 (≠ R157), K199 (≠ P187), V200 (≠ I188), M202 (= M190), C226 (≠ V215), Y228 (≠ A217), M252 (≠ V241), L253 (≠ I242)
1npdB X-ray structure of shikimate dehydrogenase complexed with NAD+ from e.Coli (ydib) northeast structural genomics research consortium (nesg) target er24 (see paper)
31% identity, 90% coverage: 25:269/272 of query aligns to 24:286/288 of 1npdB
- binding nicotinamide-adenine-dinucleotide: A132 (≠ S130), G133 (= G131), G134 (= G132), A135 (≠ M133), N155 (≠ V152), R156 (≠ A153), D158 (≠ N155), F160 (≠ R157), T204 (= T186), K205 (≠ P187), V206 (≠ I188), M208 (= M190), C232 (≠ V215), M258 (≠ V241), L259 (≠ I242)
P0A6D5 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Escherichia coli (strain K12) (see 4 papers)
31% identity, 90% coverage: 25:269/272 of query aligns to 24:286/288 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 (≠ VARN 152:155) binding
- K205 (≠ P187) binding
- CVYN 232:235 (≠ VVAI 215:218) binding
- G255 (= G238) binding
- Q262 (= Q245) 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.
1nvtB Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
31% identity, 94% coverage: 12:267/272 of query aligns to 13:281/287 of 1nvtB
- active site: K75 (= K70), D111 (= D106)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I72 (≠ M67), G135 (= G129), G137 (= G131), G138 (= G132), A139 (≠ M133), N157 (vs. gap), R158 (= R154), T159 (≠ N155), K162 (≠ A158), A200 (≠ V185), T201 (= T186), P202 (= P187), I203 (= I188), M205 (= M190), L229 (≠ V215), Y231 (≠ A217), M255 (≠ V241), L256 (≠ I242)
- binding zinc ion: E22 (vs. gap), H23 (≠ G20)
1nvtA Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
31% identity, 94% coverage: 12:267/272 of query aligns to 13:281/287 of 1nvtA
- active site: K75 (= K70), D111 (= D106)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G135 (= G129), A139 (≠ M133), N157 (vs. gap), R158 (= R154), T159 (≠ N155), K162 (≠ A158), A200 (≠ V185), T201 (= T186), P202 (= P187), I203 (= I188), M205 (= M190), L229 (≠ V215), Y231 (≠ A217), G252 (= G238), M255 (≠ V241), L256 (≠ I242)
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)
31% identity, 94% coverage: 12:267/272 of query aligns to 8:276/282 of Q58484
6hqvA Pentafunctional arom complex from chaetomium thermophilum (see paper)
27% identity, 89% coverage: 26:267/272 of query aligns to 1282:1548/1555 of 6hqvA
Sites not aligning to the query:
- active site: 123, 145, 187, 243, 253, 257, 261, 264, 268, 280
- binding (4S,5R)-4,5-dihydroxy-3-oxocyclohex-1-ene-1-carboxylic acid: 1060, 1062, 1181, 1224, 1232, 1242, 1243
- binding glutamic acid: 139, 145, 187, 243, 257, 264, 280
- binding nicotinamide-adenine-dinucleotide: 42, 44, 45, 76, 79, 107, 108, 109, 112, 132, 133, 135, 139, 140, 145, 154, 175, 176, 177, 180, 280
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: 413, 562, 563, 874, 923, 924, 979, 1277, 1279
- binding zinc ion: 187, 264, 280
Q8ZPR4 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
28% identity, 85% coverage: 25:255/272 of query aligns to 24:272/288 of Q8ZPR4
2ev9B Crystal structure of shikimate 5-dehydrogenase (aroe) from thermus thermophilus hb8 in complex with NADP(h) and shikimate (see paper)
30% identity, 89% coverage: 26:266/272 of query aligns to 19:256/263 of 2ev9B
- active site: K64 (= K70), D100 (= D106)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: N58 (≠ G64), T60 (≠ S66), K64 (= K70), N85 (= N91), D100 (= D106), Q235 (= Q245)
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)
30% identity, 89% coverage: 26:266/272 of query aligns to 19:256/263 of Q5SJF8
Sites not aligning to the query:
2cy0A Crystal structure of shikimate 5-dehydrogenase (aroe) from thermus thermophilus hb8 in complex with NADP (see paper)
30% identity, 89% coverage: 26:266/272 of query aligns to 19:256/262 of 2cy0A
- active site: K64 (= K70), D100 (= D106)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G123 (= G129), G126 (= G132), A127 (≠ M133), N146 (≠ A153), R147 (= R154), T148 (≠ N155), R151 (≠ A158), T179 (= T186), R180 (≠ P187), V181 (≠ I188), L205 (≠ V215), L232 (≠ I242)
2gptA Crystal structure of arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase in complex with tartrate and shikimate (see paper)
28% identity, 89% coverage: 27:268/272 of query aligns to 253:487/498 of 2gptA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: T292 (≠ S66), K296 (= K70), N317 (= N91), D334 (= D106), Y436 (≠ A217), Q464 (= Q245), Q468 (= Q249)
Sites not aligning to the query:
6bmqA Crystal structure of arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase (t381g mutant) in complex with tartrate and shikimate (see paper)
28% identity, 89% coverage: 27:268/272 of query aligns to 253:487/498 of 6bmqA
- binding (1S,3R,4S,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid: C291 (≠ V65), K296 (= K70), N317 (= N91), D334 (= D106), Y436 (≠ A217), Q464 (= Q245)
Sites not aligning to the query:
3tozA 2.2 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with NAD.
29% identity, 84% coverage: 26:254/272 of query aligns to 31:277/291 of 3tozA
- binding nicotinamide-adenine-dinucleotide: G137 (= G129), A138 (≠ S130), G139 (= G131), G140 (= G132), A141 (≠ M133), N161 (vs. gap), R162 (vs. gap), D164 (= D143), F166 (≠ G145), T210 (= T186), G211 (≠ P187), V212 (≠ I188), M214 (= M190), F217 (vs. gap), V238 (= V215), Y240 (≠ A217), G261 (= G238), M264 (≠ V241), M265 (≠ I242)
Q8Y9N5 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
29% identity, 84% coverage: 26:254/272 of query aligns to 31:277/291 of Q8Y9N5
Sites not aligning to the query:
Q5HNV1 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Staphylococcus epidermidis (strain ATCC 35984 / RP62A) (see paper)
24% identity, 89% coverage: 17:258/272 of query aligns to 7:252/269 of Q5HNV1
- SLS 13:15 (≠ GLR 23:25) binding
- T60 (≠ S66) binding
- N85 (= N91) binding
- D100 (= D106) binding
- Y211 (≠ A217) 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 (= Q245) binding
Query Sequence
>PfGW456L13_2490 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_2490
MQMNPNKDTQLCMSLSGRPGNFGLRFHNHLYEQLDLNFYYKAFASQDLTGAVAGIRALRI
RGCGVSMPFKEACIALVDELDASAAAIQSINTIVNTDGHLKAYNTDYIAVAQLLEKHQVP
KDSTFALRGSGGMAKAVASALRDGGYENGLIVARNERAGQALAQSLGYEWQAELGRRRPQ
MLVNVTPIGMTGGPEADQLAFEPDVIEKAETVFDVVAIPSETPLIVRARAEGKRVITGLE
VIAIQALEQFVLYTGVRPTDEQFQKAVAFARS
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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