SitesBLAST
Comparing 3608641 FitnessBrowser__Dino:3608641 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)
6an0A Crystal structure of histidinol dehydrogenase from elizabethkingia anophelis
36% identity, 94% coverage: 13:421/435 of query aligns to 24:429/433 of 6an0A
- active site: Q260 (= Q249), H263 (= H252), E327 (= E319), H328 (= H320), D361 (= D353), H420 (= H412)
- binding histidine: E103 (≠ D91), N104 (≠ T92), K105 (≠ A94), R118 (≠ Q108), E119 (≠ K109), A120 (= A110), K390 (≠ I382)
- binding zinc ion: H263 (= H252), D361 (= D353)
P10370 Histidinol dehydrogenase; HDH; EC 1.1.1.23 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
37% identity, 95% coverage: 7:420/435 of query aligns to 17:427/434 of P10370
- H99 (≠ A86) mutation to N: Slight decrease in activity.
- C117 (≠ A106) mutation C->A,S: Almost no change in activity.
- C154 (= C143) mutation C->A,S: Almost no change in activity.
- H262 (= H252) mutation to N: 7000-fold decrease in activity.
- H327 (= H320) mutation to N: 500-fold decrease in activity.
- H367 (= H360) mutation to N: Slight decrease in activity.
- H419 (= H412) mutation to Q: 20-fold decrease in activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1kaeA L-histidinol dehydrogenase (hisd) structure complexed with l- histidinol (substrate), zinc and NAD (cofactor) (see paper)
36% identity, 96% coverage: 4:420/435 of query aligns to 15:427/434 of 1kaeA
- active site: Q259 (= Q249), H262 (= H252), E326 (= E319), H327 (= H320), D360 (= D353), H419 (= H412)
- binding L-histidinol: H262 (= H252), H327 (= H320), D360 (= D353), Y361 (≠ K354), H367 (= H360)
- binding nicotinamide-adenine-dinucleotide: F58 (= F46), Y130 (= Y119), P132 (= P121), P162 (= P151), G186 (= G179), P209 (= P202), G210 (= G203), N211 (= N204), F213 (= F206), H262 (= H252)
- binding zinc ion: Q259 (= Q249), H262 (= H252), D360 (= D353)
P06988 Histidinol dehydrogenase; HDH; EC 1.1.1.23 from Escherichia coli (strain K12) (see 2 papers)
36% identity, 96% coverage: 4:420/435 of query aligns to 15:427/434 of P06988
- Y130 (= Y119) binding
- Q188 (= Q181) binding
- N211 (= N204) binding
- Q259 (= Q249) binding
- H262 (= H252) binding
- D360 (= D353) binding
- H419 (= H412) 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)
36% identity, 96% coverage: 4:420/435 of query aligns to 12:424/431 of 1karA
- active site: Q256 (= Q249), H259 (= H252), E323 (= E319), H324 (= H320), D357 (= D353), H416 (= H412)
- binding histamine: S137 (≠ A129), H259 (= H252), D357 (= D353), Y358 (≠ K354), H364 (= H360)
- binding zinc ion: H259 (= H252), D357 (= D353)
1kahA L-histidinol dehydrogenase (hisd) structure complexed with l-histidine (product), zn and NAD (cofactor) (see paper)
36% identity, 96% coverage: 4:420/435 of query aligns to 12:424/431 of 1kahA
- active site: Q256 (= Q249), H259 (= H252), E323 (= E319), H324 (= H320), D357 (= D353), H416 (= H412)
- binding histidine: L135 (≠ H127), H259 (= H252), H324 (= H320), D357 (= D353), Y358 (≠ K354), H364 (= H360), E411 (= E407), L413 (≠ M409), H416 (= H412)
- binding zinc ion: H259 (= H252), D357 (= D353)
4g09A The crystal structure of the c366s mutant of hdh from brucella suis in complex with a substituted benzyl ketone (see paper)
36% identity, 92% coverage: 19:420/435 of query aligns to 23:422/432 of 4g09A
- active site: Q253 (= Q249), H256 (= H252), E321 (= E319), H322 (= H320), D355 (= D353), H414 (= H412)
- binding (3S)-3-amino-1-[4-(benzyloxy)phenyl]-4-(1H-imidazol-4-yl)butan-2-one: P126 (= P121), A130 (≠ Y125), Y132 (≠ H127), S134 (≠ A129), H256 (= H252), E321 (= E319), H322 (= H320), D355 (= D353), Y356 (≠ K354), H362 (= H360)
- binding zinc ion: H256 (= H252), D307 (= D305), D310 (≠ E308), D355 (= D353)
5vlbA Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with imidazole (see paper)
34% identity, 94% coverage: 13:421/435 of query aligns to 21:427/434 of 5vlbA
5vldF Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidine and NAD+ (see paper)
34% identity, 94% coverage: 13:421/435 of query aligns to 22:428/435 of 5vldF
- active site: Q258 (= Q249), H261 (= H252), E326 (= E319), H327 (= H320), D360 (= D353), H419 (= H412)
- binding histidine: S135 (≠ A129), S236 (≠ T227), Q258 (= Q249), H261 (= H252), E326 (= E319), H327 (= H320), D360 (= D353), Y361 (≠ K354), H367 (= H360), E414 (= E407), H419 (= H412)
- binding nicotinamide-adenine-dinucleotide: F55 (= F46), D56 (= D47), Y125 (= Y119), P127 (= P121), G129 (= G123), T130 (≠ R124), Q187 (= Q181), P208 (= P202), G209 (= G203), N210 (= N204), Y212 (≠ F206), A233 (= A224), G234 (= G225), S236 (≠ T227), H261 (= H252), E326 (= E319), H367 (= H360), V368 (= V361), L369 (= L362)
- binding zinc ion: Q258 (= Q249), H261 (= H252), D360 (= D353)
5vlcA Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidinol (see paper)
35% identity, 92% coverage: 23:421/435 of query aligns to 29:425/431 of 5vlcA
- active site: Q255 (= Q249), H258 (= H252), E323 (= E319), H324 (= H320), D357 (= D353), H416 (= H412)
- binding L-histidinol: H258 (= H252), E323 (= E319), H324 (= H320), D357 (= D353), Y358 (≠ K354), H364 (= H360), E411 (= E407), H416 (= H412)
- binding zinc ion: Q255 (= Q249), H258 (= H252), D357 (= D353)
Query Sequence
>3608641 FitnessBrowser__Dino:3608641
MSREYLKKATLTPKSDAGETKKIVRAILDEIEAGGDDAALAYARKFDNYEGEILLSQDAI
DAAIAQVPEKLKHDIDFAHANVKRFAEAQRDTVANFEIEVVPGLIAGQKAIPVHAAGCYV
PGGRYSHIASAIMTVTTAKVAGCKHIVACSPPRPDVGIAPAIVYAAHVCGADKIMAMGGV
QGVAAMTFGLFGLPKANILVGPGNQFVAEAKRMLFGRVGIDMIAGPTDSLILADASADPM
VVAVDLVGQAEHGYNSPVWLVTDDRALAEKVMELVPGLIDDLPDVNRENATAAWRDYAEV
IVCADREEMAATSDEYAPEHLTVQAEDLDWWLERLSCYGSLFLGEETTVAFGDKASGTNH
VLPTSGAANYTGGLSVHKYMKIVTWQRSTREGSKPVALATARISRLEGMEGHARTADIRL
RKYFPDQEFDLTGND
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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