SitesBLAST
Comparing GFF492 FitnessBrowser__Marino:GFF492 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)
5eksA Structure of 3-dehydroquinate synthase from acinetobacter baumannii in complex with NAD
63% identity, 95% coverage: 6:351/364 of query aligns to 3:343/355 of 5eksA
- active site: R120 (= R121), K142 (= K143), E184 (= E185), K226 (= K227), R237 (= R241), N241 (= N245), H244 (= H248), H248 (= H252), H261 (= H265)
- binding magnesium ion: E184 (= E185), H244 (= H248), H261 (= H265)
- binding nicotinamide-adenine-dinucleotide: N42 (= N45), V45 (= V48), D71 (= D72), E73 (= E74), K76 (= K77), G104 (= G105), G105 (= G106), V106 (= V107), D109 (= D110), T129 (= T130), T130 (= T131), D136 (= D137), S137 (= S138), K142 (= K143), T172 (= T173), L173 (= L174), E177 (= E178)
U3KRF2 3-dehydroquinate synthase, chloroplastic; EC 4.2.3.4 from Actinidia chinensis var. chinensis (Chinese soft-hair kiwi) (see paper)
57% identity, 98% coverage: 8:363/364 of query aligns to 84:445/445 of U3KRF2
3zokA Structure of 3-dehydroquinate synthase from actinidia chinensis in complex with NAD (see paper)
57% identity, 98% coverage: 8:363/364 of query aligns to 4:365/365 of 3zokA
- active site: R122 (= R121), K144 (= K143), E186 (= E185), K228 (= K227), E238 (= E237), R242 (= R241), N246 (= N245), H249 (= H248), H253 (= H252), H266 (= H265)
- binding glycine: K144 (= K143), K228 (= K227), R242 (= R241)
- binding nicotinamide-adenine-dinucleotide: T44 (= T47), V45 (= V48), D73 (= D72), E75 (= E74), K78 (= K77), G106 (= G105), G107 (= G106), V108 (= V107), D111 (= D110), T131 (= T130), T132 (= T131), M134 (≠ L133), D138 (= D137), S139 (= S138), K144 (= K143), K153 (= K152), T174 (= T173), L175 (= L174), E179 (= E178), H266 (= H265)
Q9KNV2 3-dehydroquinate synthase; DHQS; EC 4.2.3.4 from Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
55% identity, 98% coverage: 6:363/364 of query aligns to 2:360/361 of Q9KNV2
3okfA 2.5 angstrom resolution crystal structure of 3-dehydroquinate synthase (arob) from vibrio cholerae
55% identity, 98% coverage: 6:363/364 of query aligns to 3:359/360 of 3okfA
- active site: R120 (= R121), K142 (= K143), E184 (= E185), K226 (= K227), R238 (= R241), N242 (= N245), H245 (= H248), H249 (= H252), H262 (= H265)
- binding nicotinamide-adenine-dinucleotide: N42 (= N45), L48 (= L51), D71 (= D72), E73 (= E74), K76 (= K77), G104 (= G105), G105 (= G106), V106 (= V107), D109 (= D110), T129 (= T130), T130 (= T131), L132 (= L133), D136 (= D137), T172 (= T173), L173 (= L174), E177 (= E178)
6llaB Crystal structure of providencia alcalifaciens 3-dehydroquinate synthase (dhqs) in complex with mg2+ and NAD (see paper)
55% identity, 94% coverage: 6:347/364 of query aligns to 3:348/363 of 6llaB
- active site: R121 (= R121), K143 (= K143), E185 (= E185), K227 (= K227), E237 (= E237), R242 (= R241), N246 (= N245), H249 (= H248), H253 (= H252), H266 (= H265)
- binding magnesium ion: E185 (= E185), H249 (= H248), H266 (= H265)
- binding nicotinamide-adenine-dinucleotide: L46 (≠ V48), D72 (= D72), E74 (= E74), K77 (= K77), G105 (= G105), G106 (= G106), V107 (= V107), D110 (= D110), T130 (= T130), T131 (= T131), L133 (= L133), D137 (= D137), K143 (= K143), T173 (= T173), L174 (= L174), E178 (= E178)
6lk2A Crystal structure of providencia alcalifaciens 3-dehydroquinate synthase (dhqs) in complex with mg2+, NAD and chlorogenic acid (see paper)
55% identity, 94% coverage: 6:347/364 of query aligns to 3:344/357 of 6lk2A
- active site: R121 (= R121), K143 (= K143), E185 (= E185), K227 (= K227), R238 (= R241), N242 (= N245), H245 (= H248), H249 (= H252), H262 (= H265)
- binding (1R,3R,4S,5R)-3-[3-[3,4-bis(oxidanyl)phenyl]propanoyloxy]-1,4,5-tris(oxidanyl)cyclohexane-1-carboxylic acid: D137 (= D137), E185 (= E185), K227 (= K227), R238 (= R241), N242 (= N245), H245 (= H248), T246 (= T249), H249 (= H252), H262 (= H265)
- binding magnesium ion: E185 (= E185), H245 (= H248), H262 (= H265)
- binding nicotinamide-adenine-dinucleotide: L46 (≠ V48), D72 (= D72), E74 (= E74), K77 (= K77), G105 (= G105), G106 (= G106), V107 (= V107), D110 (= D110), T130 (= T130), T131 (= T131), L133 (= L133), D137 (= D137), S138 (= S138), C170 (≠ S170), T173 (= T173), L174 (= L174), P175 (= P175), E178 (= E178)
Q5NFS1 3-dehydroquinate synthase; DHQS; EC 4.2.3.4 from Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
47% identity, 92% coverage: 16:351/364 of query aligns to 14:350/359 of Q5NFS1
5hvnA 3.0 angstrom crystal structure of 3-dehydroquinate synthase (arob) from francisella tularensis in complex with NAD.
46% identity, 92% coverage: 16:351/364 of query aligns to 17:345/354 of 5hvnA
- active site: R123 (= R121), K145 (= K143), E187 (= E185), K228 (= K227), R239 (= R241), N243 (= N245), H246 (= H248), H250 (= H252), H263 (= H265)
- binding nicotinamide-adenine-dinucleotide: N45 (= N45), L51 (= L51), D73 (= D72), E75 (= E74), K78 (= K77), G107 (= G105), G108 (= G106), V109 (= V107), D112 (= D110), T132 (= T130), T133 (= T131), L135 (= L133), D139 (= D137), K145 (= K143), F172 (≠ S170), T175 (= T173), L176 (= L174), E180 (= E178)
P56081 3-dehydroquinate synthase; DHQS; EC 4.2.3.4 from Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) (see paper)
41% identity, 96% coverage: 6:353/364 of query aligns to 2:335/343 of P56081
3clhA Crystal structure of 3-dehydroquinate synthase (dhqs)from helicobacter pylori (see paper)
42% identity, 81% coverage: 10:303/364 of query aligns to 3:274/308 of 3clhA
- active site: R107 (= R121), K129 (= K143), E171 (= E185), K207 (= K227), R212 (= R241), N216 (= N245), H219 (= H248), H223 (= H252), H236 (= H265)
- binding nicotinamide-adenine-dinucleotide: I33 (≠ T47), V34 (= V48), H38 (vs. gap), S58 (≠ D72), E60 (= E74), K63 (= K77), G91 (= G105), G92 (= G106), V93 (= V107), D96 (= D110), T116 (= T130), T117 (= T131), L119 (= L133), D123 (= D137), A124 (≠ S138), K129 (= K143), N139 (= N153), T159 (= T173), L160 (= L174), E164 (= E178)
6hqvA Pentafunctional arom complex from chaetomium thermophilum (see paper)
39% identity, 88% coverage: 20:340/364 of query aligns to 23:365/1555 of 6hqvA
- active site: R123 (= R121), K145 (= K143), E187 (= E185), K243 (= K227), E253 (= E237), R257 (= R241), N261 (= N245), H264 (= H248), H268 (= H252), H280 (= H265)
- binding glutamic acid: D139 (= D137), K145 (= K143), E187 (= E185), K243 (= K227), R257 (= R241), H264 (= H248), H280 (= H265)
- binding nicotinamide-adenine-dinucleotide: D42 (≠ N45), N44 (≠ T47), L45 (≠ V48), E76 (= E74), K79 (= K77), G107 (= G105), G108 (= G106), V109 (= V107), D112 (= D110), T132 (= T130), T133 (= T131), L135 (= L133), D139 (= D137), S140 (= S138), K145 (= K143), K154 (= K152), T175 (= T173), L176 (= L174), P177 (= P175), E180 (= E178), H280 (= H265)
- binding zinc ion: E187 (= E185), H264 (= H248), H280 (= H265)
Sites not aligning to the query:
- binding (4S,5R)-4,5-dihydroxy-3-oxocyclohex-1-ene-1-carboxylic acid: 1060, 1062, 1181, 1224, 1232, 1242, 1243
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: 413, 562, 563, 874, 923, 924, 979, 1277, 1279, 1323, 1327, 1348, 1368, 1526
P9WPX9 3-dehydroquinate synthase; DHQS; EC 4.2.3.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
41% identity, 95% coverage: 17:362/364 of query aligns to 18:361/362 of P9WPX9
3qbeA Crystal structure of the 3-dehydroquinate synthase (arob) from mycobacterium tuberculosis
41% identity, 95% coverage: 17:362/364 of query aligns to 13:352/352 of 3qbeA
- active site: R117 (= R121), K139 (= K143), E181 (= E185), K223 (= K227), R233 (= R241), N237 (= N245), H240 (= H248), H244 (= H252), H256 (= H265)
- binding zinc ion: E181 (= E185), H240 (= H248), H256 (= H265)
Q6GGU4 3-dehydroquinate synthase; DHQS; EC 4.2.3.4 from Staphylococcus aureus (strain MRSA252) (see paper)
35% identity, 93% coverage: 7:344/364 of query aligns to 2:334/354 of Q6GGU4
1dqsA Crystal structure of dehydroquinate synthase (dhqs) complexed with carbaphosphonate, NAD+ and zn2+ (see paper)
39% identity, 86% coverage: 29:340/364 of query aligns to 25:362/381 of 1dqsA
- active site: R127 (= R121), K149 (= K143), E191 (= E185), K240 (= K227), E250 (= E237), R254 (= R241), N258 (= N245), H261 (= H248), H265 (= H252), H277 (= H265)
- binding [1r-(1alpha,3beta,4alpha,5beta)]-5-(phosphonomethyl)-1,3,4-trihydroxycyclohexane-1-carboxylic acid: D143 (= D137), K149 (= K143), N159 (= N153), E191 (= E185), K240 (= K227), R254 (= R241), L257 (= L244), N258 (= N245), H261 (= H248), H265 (= H252), H277 (= H265), K346 (= K324)
- binding nicotinamide-adenine-dinucleotide: D41 (≠ N45), N43 (≠ T47), I44 (≠ V48), E78 (= E74), K81 (= K77), G111 (= G105), G112 (= G106), V113 (= V107), D116 (= D110), T136 (= T130), T137 (= T131), L139 (= L133), D143 (= D137), S144 (= S138), K158 (= K152), T179 (= T173), P181 (= P175), E184 (= E178), H277 (= H265)
- binding zinc ion: E191 (= E185), H261 (= H248), H277 (= H265)
1xagA Crystal structure of staphlyococcus aureus 3-dehydroquinate synthase (dhqs) in complex with zn2+, NAD+ and carbaphosphonate (see paper)
36% identity, 93% coverage: 7:344/364 of query aligns to 2:334/353 of 1xagA
- active site: R115 (= R121), K136 (= K143), E178 (= E185), K221 (= K227), E231 (= E237), R235 (= R241), N239 (= N245), H242 (= H248), H246 (= H252), H256 (= H265)
- binding [1r-(1alpha,3beta,4alpha,5beta)]-5-(phosphonomethyl)-1,3,4-trihydroxycyclohexane-1-carboxylic acid: K136 (= K143), N146 (= N153), E178 (= E185), K221 (= K227), R235 (= R241), L238 (= L244), N239 (= N245), H242 (= H248), H246 (= H252), K314 (= K324)
- binding nicotinamide-adenine-dinucleotide: D39 (≠ N45), Y41 (≠ T47), V42 (= V48), Y45 (≠ L51), E68 (= E74), K71 (= K77), G99 (= G105), G100 (= G106), A101 (≠ V107), D104 (= D110), T124 (= T130), T125 (= T131), L127 (= L133), D130 (= D137), S131 (= S138), K136 (= K143), K145 (= K152), T166 (= T173), L167 (= L174), Q171 (≠ E178), H256 (= H265)
- binding zinc ion: E178 (= E185), H242 (= H248), H256 (= H265)
1nvbB Crystal structure of 3-dehydroquinate synthase (dhqs) in complex with zn2+ and carbaphosphonate (see paper)
38% identity, 86% coverage: 29:340/364 of query aligns to 26:370/391 of 1nvbB
- active site: R128 (= R121), K150 (= K143), E192 (= E185), K248 (= K227), E258 (= E237), R262 (= R241), N266 (= N245), H269 (= H248), H273 (= H252), H285 (= H265)
- binding [1r-(1alpha,3beta,4alpha,5beta)]-5-(phosphonomethyl)-1,3,4-trihydroxycyclohexane-1-carboxylic acid: D144 (= D137), K150 (= K143), N160 (= N153), E192 (= E185), K248 (= K227), R262 (= R241), L265 (= L244), N266 (= N245), H269 (= H248), H273 (= H252), K354 (= K324)
- binding zinc ion: E192 (= E185), H269 (= H248), H285 (= H265)
P07547 Pentafunctional AROM polypeptide; EC 4.2.3.4; EC 2.5.1.19; EC 2.7.1.71; EC 4.2.1.10; EC 1.1.1.25 from Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) (see 2 papers)
38% identity, 86% coverage: 29:340/364 of query aligns to 28:372/1583 of P07547
3qbdA 3-dehydroquinate synthase (arob) from mycobacterium tuberculosis in complex with NAD
40% identity, 95% coverage: 17:362/364 of query aligns to 13:344/344 of 3qbdA
- active site: R117 (= R121), K139 (= K143), E181 (= E185), K223 (= K227), R232 (= R236), N236 (= N245), H239 (= H248), H243 (= H252), H255 (= H265)
- binding nicotinamide-adenine-dinucleotide: Q40 (≠ N45), D68 (= D72), A69 (≠ G73), E70 (= E74), K73 (= K77), G101 (= G105), G102 (= G106), A103 (≠ V107), D106 (= D110), T126 (= T130), T127 (= T131), L129 (= L133), A134 (≠ S138), T169 (= T173), L170 (= L174)
Query Sequence
>GFF492 FitnessBrowser__Marino:GFF492
MSNRYRELSVELGERSYPIFIGEGLLGTQDLSAFVSGAQVMIVTNETVAPLYLERAKACF
PGKRVDTVVLPDGEKFKDWQTLNSIFDGLLEHRHTRKTTLVALGGGVVGDMAGFAAACYQ
RGVPFIQIPTTLLSQVDSSVGGKTGINHPLGKNMIGAFHQPQAVLIDTASLQTLPAREVS
AGLAEVIKYGLIRDQGFLGWLEEHMDALVSLDPEALAEAIFRSCACKAEIVALDEREGGI
RAILNLGHTFGHAIETYAGYGNWLHGEAVGTGMLMAAELSALEGMISRDDCDRINRLILR
AGLPDKPPVAMTADDFMGLMAVDKKNVDGLLRLILLRSVGDAVVTSEASPENLALTFARF
CSST
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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