SitesBLAST
Comparing Pf6N2E2_2233 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_2233 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)
55% identity, 98% coverage: 6:272/273 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.
1npdB X-ray structure of shikimate dehydrogenase complexed with NAD+ from e.Coli (ydib) northeast structural genomics research consortium (nesg) target er24 (see paper)
32% identity, 90% coverage: 25:269/273 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 (≠ A157), 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)
32% identity, 90% coverage: 25:269/273 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.
1o9bA Quinate/shikimate dehydrogenase ydib complexed with nadh (see paper)
32% identity, 90% coverage: 25:269/273 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 (≠ A157), K199 (≠ P187), V200 (≠ I188), M202 (= M190), C226 (≠ V215), Y228 (≠ A217), M252 (≠ V241), L253 (≠ I242)
2hk9B Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
31% identity, 92% coverage: 6:255/273 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 (≠ A157), 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)
2hk9A Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
31% identity, 92% coverage: 6:255/273 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)
O67049 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Aquifex aeolicus (strain VF5) (see paper)
31% identity, 92% coverage: 6:255/273 of query aligns to 3:252/269 of O67049
1nvtB Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
32% identity, 94% coverage: 12:267/273 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 (vs. gap), T159 (vs. gap), K162 (≠ R154), 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)
32% identity, 94% coverage: 12:267/273 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 (vs. gap), T159 (vs. gap), K162 (≠ R154), 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)
32% identity, 94% coverage: 12:267/273 of query aligns to 8:276/282 of Q58484
2cy0A Crystal structure of shikimate 5-dehydrogenase (aroe) from thermus thermophilus hb8 in complex with NADP (see paper)
32% identity, 88% coverage: 26:265/273 of query aligns to 19:255/262 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)
2ev9B Crystal structure of shikimate 5-dehydrogenase (aroe) from thermus thermophilus hb8 in complex with NADP(h) and shikimate (see paper)
32% identity, 88% coverage: 26:265/273 of query aligns to 19:255/263 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)
32% identity, 88% coverage: 26:265/273 of query aligns to 19:255/263 of Q5SJF8
Sites not aligning to the query:
Q8ZPR4 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
29% identity, 90% coverage: 25:269/273 of query aligns to 24:286/288 of Q8ZPR4
- AGGA 132:135 (vs. gap) binding
- NRKD 155:158 (vs. gap) binding
- K205 (≠ P187) binding
- CVYN 232:235 (≠ TVFD 211:214) binding
- G255 (= G238) binding
6hqvA Pentafunctional arom complex from chaetomium thermophilum (see paper)
27% identity, 87% coverage: 26:262/273 of query aligns to 1282:1543/1555 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
3jyqA Quinate dehydrogenase from corynebacterium glutamicum in complex with shikimate and nadh (see paper)
30% identity, 82% coverage: 44:266/273 of query aligns to 46:278/282 of 3jyqA
- binding nicotinamide-adenine-dinucleotide: V132 (≠ R128), G135 (= G131), G136 (= G132), V137 (≠ M133), D157 (≠ G149), L158 (= L150), R162 (= R154), T201 (= T186), P202 (= P187), M205 (= M190), V227 (= V215), A254 (≠ I242)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: N66 (≠ G64), T68 (≠ S66), N93 (= N91), D109 (= D106), Q257 (= Q245)
Sites not aligning to the query:
3jypA Quinate dehydrogenase from corynebacterium glutamicum in complex with quinate and nadh (see paper)
30% identity, 82% coverage: 44:266/273 of query aligns to 46:278/282 of 3jypA
- binding nicotinamide-adenine-dinucleotide: V132 (≠ R128), G135 (= G131), V137 (≠ M133), D157 (≠ G149), L158 (= L150), R162 (= R154), T201 (= T186), P202 (= P187), M205 (= M190), A212 (= A200), V227 (= V215), Y229 (≠ A217), A254 (≠ I242)
- binding (1S,3R,4S,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid: N66 (≠ G64), T68 (≠ S66), K72 (= K70), N93 (= N91), D109 (= D106), Q257 (= Q245)
Sites not aligning to the query:
3jyoA Quinate dehydrogenase from corynebacterium glutamicum in complex with NAD (see paper)
30% identity, 82% coverage: 44:266/273 of query aligns to 46:278/282 of 3jyoA
- binding nicotinamide-adenine-dinucleotide: V132 (≠ R128), G135 (= G131), V137 (≠ M133), D157 (≠ G149), L158 (= L150), R162 (= R154), T201 (= T186), P202 (= P187), M205 (= M190), V227 (= V215), Y229 (≠ A217), A254 (≠ I242)
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)
30% identity, 82% coverage: 44:266/273 of query aligns to 47:279/283 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 (≠ G149) binding
- R163 (= R154) binding
- PMGM 203:206 (≠ PIGM 187:190) binding
- A213 (= A200) binding
- V228 (= V215) binding
- G251 (= G238) binding
- Q258 (= Q245) binding ; binding
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: 26:254/273 of query aligns to 31:277/291 of 3tozA
- binding nicotinamide-adenine-dinucleotide: G137 (≠ L127), A138 (≠ R128), G139 (= G129), G140 (≠ S130), A141 (≠ G131), 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)
Query Sequence
>Pf6N2E2_2233 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_2233
MQINPNKDTQLCMSLSGRPGNFGLRFHNHLYEQLGLNFYYKAFSSQDLPGAVGGIRALGI
RGCGVSMPFKEACIALVDELDPSAAAIESINTIVNTNGHLKAYNTDYIAIAQLLQSHAVP
KDSTFALRGSGGMAKAVASALRDGGYQNGLIVARNEAAGRALAESLGYEWQADLGTRRPQ
MLINVTPIGMTGGPEADQLAFEPETIVAAETVFDVVAIPSETPLIVRARAEGKRVITGLE
VIAIQALEQFVLYTGVRPNLEQFEKTVTFARSA
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