SitesBLAST
Comparing WP_051243133.1 NCBI__GCF_000430725.1:WP_051243133.1 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)
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)
47% identity, 94% coverage: 12:290/296 of query aligns to 2:283/283 of Q9X5C9
- S17 (= S27) binding
- SRT 17:19 (≠ SLT 27:29) binding
- T69 (= T79) binding ; binding
- K73 (= K83) active site, Proton acceptor; binding ; binding
- N94 (= N104) binding ; binding
- D110 (= D119) binding ; binding
- GV 137:138 (≠ GA 146:147) binding
- D158 (= D167) binding
- R163 (= R172) binding
- PMGM 203:206 (= PMGM 210:213) binding
- A213 (≠ P220) binding
- V228 (= V235) binding
- G251 (= G258) binding
- Q258 (= Q265) binding ; binding
3jyqA Quinate dehydrogenase from corynebacterium glutamicum in complex with shikimate and nadh (see paper)
47% identity, 94% coverage: 12:290/296 of query aligns to 1:282/282 of 3jyqA
- binding nicotinamide-adenine-dinucleotide: V132 (≠ L142), G135 (= G145), G136 (= G146), V137 (≠ A147), D157 (= D167), L158 (≠ V168), R162 (= R172), T201 (= T209), P202 (= P210), M205 (= M213), V227 (= V235), A254 (= A262)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S16 (= S27), N66 (= N77), T68 (= T79), N93 (= N104), D109 (= D119), Q257 (= Q265)
3jypA Quinate dehydrogenase from corynebacterium glutamicum in complex with quinate and nadh (see paper)
47% identity, 94% coverage: 12:290/296 of query aligns to 1:282/282 of 3jypA
- binding nicotinamide-adenine-dinucleotide: V132 (≠ L142), G135 (= G145), V137 (≠ A147), D157 (= D167), L158 (≠ V168), R162 (= R172), T201 (= T209), P202 (= P210), M205 (= M213), A212 (≠ P220), V227 (= V235), Y229 (= Y237), A254 (= A262)
- binding (1S,3R,4S,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid: S16 (= S27), T18 (= T29), N66 (= N77), T68 (= T79), K72 (= K83), N93 (= N104), D109 (= D119), Q257 (= Q265)
3jyoA Quinate dehydrogenase from corynebacterium glutamicum in complex with NAD (see paper)
47% identity, 94% coverage: 12:290/296 of query aligns to 1:282/282 of 3jyoA
- binding nicotinamide-adenine-dinucleotide: V132 (≠ L142), G135 (= G145), V137 (≠ A147), D157 (= D167), L158 (≠ V168), R162 (= R172), T201 (= T209), P202 (= P210), M205 (= M213), V227 (= V235), Y229 (= Y237), A254 (= A262)
3tozA 2.2 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with NAD.
34% identity, 94% coverage: 1:277/296 of query aligns to 1:280/291 of 3tozA
- binding nicotinamide-adenine-dinucleotide: G137 (= G143), A138 (≠ T144), G139 (= G145), G140 (= G146), A141 (= A147), N161 (vs. gap), R162 (vs. gap), D164 (= D167), F166 (≠ D169), T210 (= T209), G211 (≠ P210), V212 (≠ M211), M214 (= M213), F217 (≠ M216), V238 (= V235), Y240 (= Y237), G261 (= G258), M264 (= M261), M265 (≠ A262)
Q8Y9N5 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
34% identity, 94% coverage: 1:277/296 of query aligns to 1:280/291 of Q8Y9N5
3tnlA 1.45 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with shikimate and NAD.
34% identity, 89% coverage: 16:277/296 of query aligns to 12:277/288 of 3tnlA
- binding nicotinamide-adenine-dinucleotide: M71 (≠ F80), G134 (= G143), A135 (≠ T144), G136 (= G145), G137 (= G146), A138 (= A147), N158 (vs. gap), R159 (vs. gap), D161 (= D167), F163 (≠ D169), T207 (= T209), V209 (≠ M211), M211 (= M213), F214 (≠ M216), V235 (= V235), Y237 (= Y237), M261 (= M261), M262 (≠ A262)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S23 (= S27), S25 (≠ T29), N68 (= N77), S70 (≠ T79), K74 (= K83), N95 (= N104), D110 (= D119), Q265 (= Q265)
Q5HNV1 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Staphylococcus epidermidis (strain ATCC 35984 / RP62A) (see paper)
30% identity, 88% coverage: 19:279/296 of query aligns to 5:253/269 of Q5HNV1
- SLS 13:15 (≠ SLT 27:29) binding
- T60 (= T79) binding
- N85 (= N104) binding
- D100 (= D119) binding
- Y211 (= Y237) 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 (= Q265) binding
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, 89% coverage: 16:277/296 of query aligns to 9:274/288 of 1npdB
- binding nicotinamide-adenine-dinucleotide: A132 (≠ T144), G133 (= G145), G134 (= G146), A135 (= A147), N155 (vs. gap), R156 (vs. gap), D158 (= D167), F160 (≠ D169), T204 (= T209), K205 (≠ P210), V206 (≠ M211), M208 (= M213), C232 (≠ V235), M258 (= M261), L259 (≠ A262)
P0A6D5 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Escherichia coli (strain K12) (see 4 papers)
32% identity, 89% coverage: 16:277/296 of query aligns to 9:274/288 of P0A6D5
- S22 (≠ T29) mutation to A: Kinetically unchanged as compared with the wild-type.
- Y39 (= Y46) mutation to F: Kinetically unchanged as compared with the wild-type.
- S67 (≠ T79) mutation to A: Reduces activity towards quinate about 6-fold, but has a little effect on shikimate conversion.
- K71 (= K83) 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 (= N104) mutation to A: Alters protein structure. Loss of activity for both substrates.
- T106 (= T118) 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 (= D119) mutation to A: Loss of activity towards quinate. 20000-fold decrease in the affinity for shikimate.
- AGGA 132:135 (≠ TGGA 144:147) binding
- NRRD 155:158 (≠ ---D 167) binding
- K205 (≠ P210) binding
- CVYN 232:235 (≠ VVYF 235:238) binding
- G255 (= G258) binding
- Q262 (= Q265) mutation to A: 3-fold reduction in catalytic efficiency for both substrates.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1o9bA Quinate/shikimate dehydrogenase ydib complexed with nadh (see paper)
32% identity, 89% coverage: 16:277/296 of query aligns to 3:268/280 of 1o9bA
- binding 1,4-dihydronicotinamide adenine dinucleotide: A126 (≠ T144), G127 (= G145), G128 (= G146), A129 (= A147), R150 (vs. gap), F154 (≠ D169), K199 (≠ P210), V200 (≠ M211), M202 (= M213), C226 (≠ V235), Y228 (= Y237), M252 (= M261), L253 (≠ A262)
O67049 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Aquifex aeolicus (strain VF5) (see paper)
30% identity, 89% coverage: 16:277/296 of query aligns to 8:254/269 of O67049
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, 89% coverage: 16:279/296 of query aligns to 8:268/282 of Q58484
1nvtB Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
31% identity, 89% coverage: 16:279/296 of query aligns to 13:273/287 of 1nvtB
- active site: K75 (= K83), D111 (= D119)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I72 (≠ F80), G135 (= G143), G137 (= G145), G138 (= G146), A139 (= A147), N157 (≠ L163), R158 (= R164), T159 (≠ L165), K162 (≠ V168), A200 (= A208), T201 (= T209), P202 (= P210), I203 (≠ M211), M205 (= M213), L229 (≠ V235), Y231 (= Y237), M255 (= M261), L256 (≠ A262)
- binding zinc ion: E22 (≠ Q25), H23 (≠ R26)
1nvtA Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
31% identity, 89% coverage: 16:279/296 of query aligns to 13:273/287 of 1nvtA
- active site: K75 (= K83), D111 (= D119)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G135 (= G143), A139 (= A147), N157 (≠ L163), R158 (= R164), T159 (≠ L165), K162 (≠ V168), A200 (= A208), T201 (= T209), P202 (= P210), I203 (≠ M211), M205 (= M213), L229 (≠ V235), Y231 (= Y237), G252 (= G258), M255 (= M261), L256 (≠ A262)
2hk9B Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
30% identity, 89% coverage: 16:277/296 of query aligns to 8:254/267 of 2hk9B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V67 (≠ F80), G130 (= G143), G133 (= G146), A134 (= A147), N153 (≠ D167), R154 (≠ V168), T155 (≠ D169), K158 (≠ R172), T188 (= T209), S189 (≠ P210), V190 (≠ M211), I214 (≠ V235), M238 (= M261), L239 (≠ A262)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S27), S21 (≠ T29), N64 (= N77), T66 (= T79), K70 (= K83), N91 (= N104), D106 (= D119), Y216 (= Y237), L239 (≠ A262), Q242 (= Q265)
2hk9A Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
30% identity, 89% coverage: 16:277/296 of query aligns to 8:254/269 of 2hk9A
- binding 2'-monophosphoadenosine-5'-diphosphate: V67 (≠ F80), G132 (= G145), G133 (= G146), A134 (= A147), N153 (≠ D167), R154 (≠ V168), T155 (≠ D169), T188 (= T209), S189 (≠ P210), V190 (≠ M211)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S27), S21 (≠ T29), N64 (= N77), K70 (= K83), N91 (= N104), D106 (= D119), Y216 (= Y237), L239 (≠ A262), Q242 (= Q265)
3dooA Crystal structure of shikimate dehydrogenase from staphylococcus epidermidis complexed with shikimate (see paper)
29% identity, 88% coverage: 19:279/296 of query aligns to 5:244/258 of 3dooA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S13 (= S27), S15 (≠ T29), N58 (= N77), T60 (= T79), K64 (= K83), N85 (= N104), D100 (= D119), F227 (≠ A262), Q230 (= Q265)
Q8ZPR4 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
33% identity, 88% coverage: 16:276/296 of query aligns to 9:273/288 of Q8ZPR4
7colA Crystal structure of 5-ketofructose reductase complexed with NADPH (see paper)
35% identity, 91% coverage: 14:281/296 of query aligns to 5:268/280 of 7colA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G128 (≠ L142), G130 (≠ T144), G131 (= G145), A132 (≠ G146), N152 (≠ D167), R153 (≠ V168), K157 (≠ R172), T195 (= T209), S196 (≠ P210), I197 (≠ M211), V222 (= V235), Q252 (= Q265)
Query Sequence
>WP_051243133.1 NCBI__GCF_000430725.1:WP_051243133.1
MTASSTPMAFPHNKLLVGLIGAGIQRSLTPAMQEEEARHHGLRMHYQLIDLDTTQSGPEL
LPTLLAAVRTMGFAGLNITFPCKQAVIPLLDDLSDEARAMGAVNTVVHRDGKLIGHNTDG
SGWSWNFQRQLPDADLSRVLLLGTGGAGSAIAHAALRMGVQELRLFDVDPARAEGLAAEL
NRLYGAGRAVAAADIAGGIADATGLIHATPMGMDKMPGLPLAEELLRPELWVSEVVYFPI
DTALLKAARAKGCPTVDGGGMAVGQAVGAFKLFTGREPDAARIDAHFRRLLAERAA
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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