SitesBLAST
Comparing 16128 FitnessBrowser__Keio:16128 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 10 hits to proteins with known functional sites (download)
1kaeA L-histidinol dehydrogenase (hisd) structure complexed with l- histidinol (substrate), zinc and NAD (cofactor) (see paper)
100% identity, 100% coverage: 1:434/434 of query aligns to 1:434/434 of 1kaeA
- active site: Q259 (= Q259), H262 (= H262), E326 (= E326), H327 (= H327), D360 (= D360), H419 (= H419)
- binding L-histidinol: H262 (= H262), H327 (= H327), D360 (= D360), Y361 (= Y361), H367 (= H367)
- binding nicotinamide-adenine-dinucleotide: F58 (= F58), Y130 (= Y130), P132 (= P132), P162 (= P162), G186 (= G186), P209 (= P209), G210 (= G210), N211 (= N211), F213 (= F213), H262 (= H262)
- binding zinc ion: Q259 (= Q259), H262 (= H262), D360 (= D360)
P06988 Histidinol dehydrogenase; HDH; EC 1.1.1.23 from Escherichia coli (strain K12) (see 2 papers)
100% identity, 100% coverage: 1:434/434 of query aligns to 1:434/434 of P06988
- M1 (= M1) modified: Initiator methionine, Removed
- Y130 (= Y130) binding
- Q188 (= Q188) binding
- N211 (= N211) binding
- Q259 (= Q259) binding
- H262 (= H262) binding
- D360 (= D360) binding
- H419 (= H419) binding
1karA L-histidinol dehydrogenase (hisd) structure complexed with histamine (inhibitor), zinc and NAD (cofactor) (see paper)
100% identity, 99% coverage: 4:434/434 of query aligns to 1:431/431 of 1karA
- active site: Q256 (= Q259), H259 (= H262), E323 (= E326), H324 (= H327), D357 (= D360), H416 (= H419)
- binding histamine: S137 (= S140), H259 (= H262), D357 (= D360), Y358 (= Y361), H364 (= H367)
- binding zinc ion: H259 (= H262), D357 (= D360)
1kahA L-histidinol dehydrogenase (hisd) structure complexed with l-histidine (product), zn and NAD (cofactor) (see paper)
100% identity, 99% coverage: 4:434/434 of query aligns to 1:431/431 of 1kahA
- active site: Q256 (= Q259), H259 (= H262), E323 (= E326), H324 (= H327), D357 (= D360), H416 (= H419)
- binding histidine: L135 (= L138), H259 (= H262), H324 (= H327), D357 (= D360), Y358 (= Y361), H364 (= H367), E411 (= E414), L413 (= L416), H416 (= H419)
- binding zinc ion: H259 (= H262), D357 (= D360)
P10370 Histidinol dehydrogenase; HDH; EC 1.1.1.23 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
92% identity, 100% coverage: 1:434/434 of query aligns to 1:434/434 of P10370
- M1 (= M1) modified: Initiator methionine, Removed
- H99 (= H99) mutation to N: Slight decrease in activity.
- C117 (= C117) mutation C->A,S: Almost no change in activity.
- C154 (= C154) mutation C->A,S: Almost no change in activity.
- H262 (= H262) mutation to N: 7000-fold decrease in activity.
- H327 (= H327) mutation to N: 500-fold decrease in activity.
- H367 (= H367) mutation to N: Slight decrease in activity.
- H419 (= H419) mutation to Q: 20-fold decrease in activity.
6an0A Crystal structure of histidinol dehydrogenase from elizabethkingia anophelis
51% identity, 96% coverage: 16:431/434 of query aligns to 16:432/433 of 6an0A
- active site: Q260 (= Q259), H263 (= H262), E327 (= E326), H328 (= H327), D361 (= D360), H420 (= H419)
- binding histidine: E103 (≠ L104), N104 (≠ P105), K105 (≠ P106), R118 (≠ Q119), E119 (≠ V120), A120 (≠ T121), K390 (≠ R389)
- binding zinc ion: H263 (= H262), D361 (= D360)
5vlbA Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with imidazole (see paper)
50% identity, 94% coverage: 23:431/434 of query aligns to 20:430/434 of 5vlbA
5vldF Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidine and NAD+ (see paper)
50% identity, 94% coverage: 23:431/434 of query aligns to 21:431/435 of 5vldF
- active site: Q258 (= Q259), H261 (= H262), E326 (= E326), H327 (= H327), D360 (= D360), H419 (= H419)
- binding histidine: S135 (= S140), S236 (= S237), Q258 (= Q259), H261 (= H262), E326 (= E326), H327 (= H327), D360 (= D360), Y361 (= Y361), H367 (= H367), E414 (= E414), H419 (= H419)
- binding nicotinamide-adenine-dinucleotide: F55 (= F58), D56 (= D59), Y125 (= Y130), P127 (= P132), G129 (= G134), T130 (≠ S135), Q187 (= Q188), P208 (= P209), G209 (= G210), N210 (= N211), Y212 (≠ F213), A233 (= A234), G234 (= G235), S236 (= S237), H261 (= H262), E326 (= E326), H367 (= H367), V368 (= V368), L369 (= L369)
- binding zinc ion: Q258 (= Q259), H261 (= H262), D360 (= D360)
5vlcA Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidinol (see paper)
50% identity, 95% coverage: 20:431/434 of query aligns to 18:428/431 of 5vlcA
- active site: Q255 (= Q259), H258 (= H262), E323 (= E326), H324 (= H327), D357 (= D360), H416 (= H419)
- binding L-histidinol: H258 (= H262), E323 (= E326), H324 (= H327), D357 (= D360), Y358 (= Y361), H364 (= H367), E411 (= E414), H416 (= H419)
- binding zinc ion: Q255 (= Q259), H258 (= H262), D357 (= D360)
4g09A The crystal structure of the c366s mutant of hdh from brucella suis in complex with a substituted benzyl ketone (see paper)
42% identity, 94% coverage: 25:431/434 of query aligns to 17:426/432 of 4g09A
- active site: Q253 (= Q259), H256 (= H262), E321 (= E326), H322 (= H327), D355 (= D360), H414 (= H419)
- binding (3S)-3-amino-1-[4-(benzyloxy)phenyl]-4-(1H-imidazol-4-yl)butan-2-one: P126 (= P132), A130 (= A136), Y132 (≠ L138), S134 (= S140), H256 (= H262), E321 (= E326), H322 (= H327), D355 (= D360), Y356 (= Y361), H362 (= H367)
- binding zinc ion: H256 (= H262), D307 (= D312), D310 (≠ Q315), D355 (= D360)
Query Sequence
>16128 FitnessBrowser__Keio:16128
MSFNTIIDWNSCTAEQQRQLLMRPAISASESITRTVNDILDNVKARGDEALREYSAKFDK
TTVTALKVSAEEIAAASERLSDELKQAMAVAVKNIETFHTAQKLPPVDVETQPGVRCQQV
TRPVASVGLYIPGGSAPLFSTVLMLATPASIAGCKKVVLCSPPPIADEILYAAQLCGVQD
VFNVGGAQAIAALAFGTESVPKVDKIFGPGNAFVTEAKRQVSQRLDGAAIDMPAGPSEVL
VIADSGATPDFVASDLLSQAEHGPDSQVILLTPAADMARRVAEAVERQLAELPRAETARQ
ALNASRLIVTKDLAQCVEISNQYGPEHLIIQTRNARELVDSITSAGSVFLGDWSPESAGD
YASGTNHVLPTYGYTATCSSLGLADFQKRMTVQELSKEGFSALASTIETLAAAERLTAHK
NAVTLRVNALKEQA
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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