SitesBLAST
Comparing SMc02307 FitnessBrowser__Smeli:SMc02307 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)
4g09A The crystal structure of the c366s mutant of hdh from brucella suis in complex with a substituted benzyl ketone (see paper)
75% identity, 99% coverage: 5:432/434 of query aligns to 4:426/432 of 4g09A
- active site: Q253 (= Q259), H256 (= H262), E321 (= E327), H322 (= H328), D355 (= D361), H414 (= H420)
- binding (3S)-3-amino-1-[4-(benzyloxy)phenyl]-4-(1H-imidazol-4-yl)butan-2-one: P126 (= P132), A130 (= A136), Y132 (= Y138), S134 (= S140), H256 (= H262), E321 (= E327), H322 (= H328), D355 (= D361), Y356 (= Y362), H362 (= H368)
- binding zinc ion: H256 (= H262), D307 (= D313), D310 (≠ K316), D355 (= D361)
1kaeA L-histidinol dehydrogenase (hisd) structure complexed with l- histidinol (substrate), zinc and NAD (cofactor) (see paper)
44% identity, 94% coverage: 27:433/434 of query aligns to 29:432/434 of 1kaeA
- active site: Q259 (= Q259), H262 (= H262), E326 (= E327), H327 (= H328), D360 (= D361), H419 (= H420)
- binding L-histidinol: H262 (= H262), H327 (= H328), D360 (= D361), Y361 (= Y362), H367 (= H368)
- binding nicotinamide-adenine-dinucleotide: F58 (= F56), Y130 (= Y130), P132 (= P132), P162 (= P162), G186 (= G189), P209 (= P212), G210 (= G213), N211 (= N214), F213 (≠ Y216), H262 (= H262)
- binding zinc ion: Q259 (= Q259), H262 (= H262), D360 (= D361)
P06988 Histidinol dehydrogenase; HDH; EC 1.1.1.23 from Escherichia coli (strain K12) (see 2 papers)
44% identity, 94% coverage: 27:433/434 of query aligns to 29:432/434 of P06988
- Y130 (= Y130) binding
- Q188 (= Q191) binding
- N211 (= N214) binding
- Q259 (= Q259) binding
- H262 (= H262) binding
- D360 (= D361) binding
- H419 (= H420) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1karA L-histidinol dehydrogenase (hisd) structure complexed with histamine (inhibitor), zinc and NAD (cofactor) (see paper)
44% identity, 94% coverage: 27:433/434 of query aligns to 26:429/431 of 1karA
- active site: Q256 (= Q259), H259 (= H262), E323 (= E327), H324 (= H328), D357 (= D361), H416 (= H420)
- binding histamine: S137 (= S140), H259 (= H262), D357 (= D361), Y358 (= Y362), H364 (= H368)
- binding zinc ion: H259 (= H262), D357 (= D361)
1kahA L-histidinol dehydrogenase (hisd) structure complexed with l-histidine (product), zn and NAD (cofactor) (see paper)
44% identity, 94% coverage: 27:433/434 of query aligns to 26:429/431 of 1kahA
- active site: Q256 (= Q259), H259 (= H262), E323 (= E327), H324 (= H328), D357 (= D361), H416 (= H420)
- binding histidine: L135 (≠ Y138), H259 (= H262), H324 (= H328), D357 (= D361), Y358 (= Y362), H364 (= H368), E411 (= E415), L413 (= L417), H416 (= H420)
- binding zinc ion: H259 (= H262), D357 (= D361)
6an0A Crystal structure of histidinol dehydrogenase from elizabethkingia anophelis
40% identity, 93% coverage: 27:428/434 of query aligns to 28:428/433 of 6an0A
- active site: Q260 (= Q259), H263 (= H262), E327 (= E327), H328 (= H328), D361 (= D361), H420 (= H420)
- binding histidine: E103 (≠ P104), N104 (≠ K105), K105 (≠ D106), R118 (≠ S119), E119 (≠ R120), A120 (≠ W121), K390 (≠ R390)
- binding zinc ion: H263 (= H262), D361 (= D361)
P10370 Histidinol dehydrogenase; HDH; EC 1.1.1.23 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
44% identity, 94% coverage: 27:433/434 of query aligns to 29:432/434 of P10370
- H99 (= H99) mutation to N: Slight decrease in activity.
- C117 (≠ L117) mutation C->A,S: Almost no change in activity.
- C154 (≠ V154) mutation C->A,S: Almost no change in activity.
- H262 (= H262) mutation to N: 7000-fold decrease in activity.
- H327 (= H328) mutation to N: 500-fold decrease in activity.
- H367 (= H368) mutation to N: Slight decrease in activity.
- H419 (= H420) mutation to Q: 20-fold decrease in activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5vlbA Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with imidazole (see paper)
40% identity, 98% coverage: 3:429/434 of query aligns to 1:427/434 of 5vlbA
5vldF Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidine and NAD+ (see paper)
40% identity, 98% coverage: 3:429/434 of query aligns to 2:428/435 of 5vldF
- active site: Q258 (= Q259), H261 (= H262), E326 (= E327), H327 (= H328), D360 (= D361), H419 (= H420)
- binding histidine: S135 (= S140), S236 (= S237), Q258 (= Q259), H261 (= H262), E326 (= E327), H327 (= H328), D360 (= D361), Y361 (= Y362), H367 (= H368), E414 (= E415), H419 (= H420)
- binding nicotinamide-adenine-dinucleotide: F55 (= F56), D56 (= D57), Y125 (= Y130), P127 (= P132), G129 (= G134), T130 (= T135), Q187 (= Q191), P208 (= P212), G209 (= G213), N210 (= N214), Y212 (= Y216), A233 (= A234), G234 (= G235), S236 (= S237), H261 (= H262), E326 (= E327), H367 (= H368), V368 (= V369), L369 (= L370)
- binding zinc ion: Q258 (= Q259), H261 (= H262), D360 (= D361)
5vlcA Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidinol (see paper)
42% identity, 91% coverage: 33:429/434 of query aligns to 29:425/431 of 5vlcA
- active site: Q255 (= Q259), H258 (= H262), E323 (= E327), H324 (= H328), D357 (= D361), H416 (= H420)
- binding L-histidinol: H258 (= H262), E323 (= E327), H324 (= H328), D357 (= D361), Y358 (= Y362), H364 (= H368), E411 (= E415), H416 (= H420)
- binding zinc ion: Q255 (= Q259), H258 (= H262), D357 (= D361)
Query Sequence
>SMc02307 FitnessBrowser__Smeli:SMc02307
MAIRLNYLDTSFERDFAAFLTTKREVSEDVNAVVRAIIDDVRARGDAALADYSARFDGID
FTVTGMAVTSAEIDAAIHAVAPEVLGALKVAATRIEAHHRRQLPKDDIYEDQMGVGLGSR
WTPIDAVGLYVPGGTASYPSSVLMNALPAKVAGVPRIVMVVPASGGSINPAVLAAARLAG
VEEIYRIGGAQAVAALAYGTETIEPVAKIVGPGNAYVAAAKRQVFGTVGIDMIAGPSEVL
VIADRDNDPDWIAADLLAQAEHDAGAQAILITDDAAFGDAVEKAVERQLKTLPRAETAAA
SWRDFGAVILVPDFDKAVPLANRIAPEHLELATADPDAMVPAIRNAGAIFIGRHTPEVIG
DYVGGSNHVLPTARSARFSSGLGVLDYVKRTSILRLGPDQLRILGPAAIALARSEGLEAH
ARSVAIRLNLGEEG
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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