SitesBLAST
Comparing N515DRAFT_2937 FitnessBrowser__Dyella79:N515DRAFT_2937 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)
1karA L-histidinol dehydrogenase (hisd) structure complexed with histamine (inhibitor), zinc and NAD (cofactor) (see paper)
59% identity, 99% coverage: 4:435/435 of query aligns to 4:431/431 of 1karA
- active site: Q256 (= Q260), H259 (= H263), E323 (= E327), H324 (= H328), D357 (= D361), H416 (= H420)
- binding histamine: S137 (= S137), H259 (= H263), D357 (= D361), Y358 (= Y362), H364 (= H368)
- binding zinc ion: H259 (= H263), D357 (= D361)
1kahA L-histidinol dehydrogenase (hisd) structure complexed with l-histidine (product), zn and NAD (cofactor) (see paper)
59% identity, 99% coverage: 4:435/435 of query aligns to 4:431/431 of 1kahA
- active site: Q256 (= Q260), H259 (= H263), E323 (= E327), H324 (= H328), D357 (= D361), H416 (= H420)
- binding histidine: L135 (= L135), H259 (= H263), H324 (= H328), D357 (= D361), Y358 (= Y362), H364 (= H368), E411 (= E415), L413 (= L417), H416 (= H420)
- binding zinc ion: H259 (= H263), D357 (= D361)
1kaeA L-histidinol dehydrogenase (hisd) structure complexed with l- histidinol (substrate), zinc and NAD (cofactor) (see paper)
59% identity, 99% coverage: 4:435/435 of query aligns to 7:434/434 of 1kaeA
- active site: Q259 (= Q260), H262 (= H263), E326 (= E327), H327 (= H328), D360 (= D361), H419 (= H420)
- binding L-histidinol: H262 (= H263), H327 (= H328), D360 (= D361), Y361 (= Y362), H367 (= H368)
- binding nicotinamide-adenine-dinucleotide: F58 (≠ Y55), Y130 (= Y127), P132 (= P129), P162 (= P159), G186 (= G187), P209 (= P210), G210 (= G211), N211 (= N212), F213 (≠ W214), H262 (= H263)
- binding zinc ion: Q259 (= Q260), H262 (= H263), D360 (= D361)
P06988 Histidinol dehydrogenase; HDH; EC 1.1.1.23 from Escherichia coli (strain K12) (see 2 papers)
59% identity, 99% coverage: 4:435/435 of query aligns to 7:434/434 of P06988
- Y130 (= Y127) binding
- Q188 (= Q189) binding
- N211 (= N212) binding
- Q259 (= Q260) binding
- H262 (= H263) binding
- D360 (= D361) binding
- H419 (= H420) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
P10370 Histidinol dehydrogenase; HDH; EC 1.1.1.23 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
58% identity, 99% coverage: 4:435/435 of query aligns to 7:434/434 of P10370
- H99 (= H96) mutation to N: Slight decrease in activity.
- C117 (≠ V114) mutation C->A,S: Almost no change in activity.
- C154 (= C151) mutation C->A,S: Almost no change in activity.
- H262 (= H263) 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
6an0A Crystal structure of histidinol dehydrogenase from elizabethkingia anophelis
50% identity, 96% coverage: 18:433/435 of query aligns to 21:433/433 of 6an0A
- active site: Q260 (= Q260), H263 (= H263), E327 (= E327), H328 (= H328), D361 (= D361), H420 (= H420)
- binding histidine: E103 (≠ P101), N104 (≠ R102), K105 (≠ P103), R118 (= R116), E119 (≠ V117), A120 (≠ L118), K390 (≠ Q390)
- binding zinc ion: H263 (= H263), D361 (= D361)
5vlbA Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with imidazole (see paper)
52% identity, 92% coverage: 33:434/435 of query aligns to 32:432/434 of 5vlbA
5vldF Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidine and NAD+ (see paper)
52% identity, 92% coverage: 33:434/435 of query aligns to 33:433/435 of 5vldF
- active site: Q258 (= Q260), H261 (= H263), E326 (= E327), H327 (= H328), D360 (= D361), H419 (= H420)
- binding histidine: S135 (= S137), S236 (= S238), Q258 (= Q260), H261 (= H263), E326 (= E327), H327 (= H328), D360 (= D361), Y361 (= Y362), H367 (= H368), E414 (= E415), H419 (= H420)
- binding nicotinamide-adenine-dinucleotide: F55 (≠ Y55), D56 (= D56), Y125 (= Y127), P127 (= P129), G129 (= G131), T130 (≠ S132), Q187 (= Q189), P208 (= P210), G209 (= G211), N210 (= N212), Y212 (≠ W214), A233 (= A235), G234 (= G236), S236 (= S238), H261 (= H263), E326 (= E327), H367 (= H368), V368 (= V369), L369 (= L370)
- binding zinc ion: Q258 (= Q260), H261 (= H263), D360 (= D361)
5vlcA Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidinol (see paper)
52% identity, 92% coverage: 33:434/435 of query aligns to 30:430/431 of 5vlcA
- active site: Q255 (= Q260), H258 (= H263), E323 (= E327), H324 (= H328), D357 (= D361), H416 (= H420)
- binding L-histidinol: H258 (= H263), E323 (= E327), H324 (= H328), D357 (= D361), Y358 (= Y362), H364 (= H368), E411 (= E415), H416 (= H420)
- binding zinc ion: Q255 (= Q260), H258 (= H263), D357 (= D361)
4g09A The crystal structure of the c366s mutant of hdh from brucella suis in complex with a substituted benzyl ketone (see paper)
42% identity, 93% coverage: 27:432/435 of query aligns to 22:426/432 of 4g09A
- active site: Q253 (= Q260), H256 (= H263), 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 (= P129), A130 (= A133), Y132 (≠ L135), S134 (= S137), H256 (= H263), E321 (= E327), H322 (= H328), D355 (= D361), Y356 (= Y362), H362 (= H368)
- binding zinc ion: H256 (= H263), D307 (≠ S313), D310 (≠ Q316), D355 (= D361)
Query Sequence
>N515DRAFT_2937 FitnessBrowser__Dyella79:N515DRAFT_2937
MKRLDWNALDPAAQLQALARPAQSRAEELRRGVEAIVAKVRAEGDTALRELSAKYDRCAI
DAIEVTVEEFAAAEAALAPELKAAIEEAAARIAAFHRESAPRPVAVETAPGVRVERVLRP
IAKVGLYVPAGSAPLPSTALMLGVPAGLAGCREVVLCSPARADGRCDEAVLYAARVTGVH
RVFKLGGAQAIAAMAYGTGSVPRCDKLFGPGNAWVTEAKLQVSGDPDGAAIDMPAGPSEV
LVIADGKADPEFVAADLLSQAEHGPDSQVILLSPSDALLDRVAVEVERQCAALPRASIAT
QALAQSRLILVDSLAQAVAVSNRYAPEHLILQVTEPRALLDGIDSAGSIFLGAWTPESVG
DYCSGSNHVLPTYGYARSYSGVSVASFQKQITVQELSADGLRAIGPCTATLAEAEQLEAH
RRAVTLRLAALEARA
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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