SitesBLAST
Comparing Echvi_2459 FitnessBrowser__Cola:Echvi_2459 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 10 hits to proteins with known functional sites (download)
6an0A Crystal structure of histidinol dehydrogenase from elizabethkingia anophelis
59% identity, 99% coverage: 1:426/429 of query aligns to 6:431/433 of 6an0A
- active site: Q260 (= Q255), H263 (= H258), E327 (= E322), H328 (= H323), D361 (= D356), H420 (= H415)
- binding histidine: E103 (≠ T98), N104 (≠ E99), K105 (≠ D100), R118 (= R113), E119 (≠ R114), A120 (≠ S115), K390 (= K385)
- binding zinc ion: H263 (= H258), D361 (= D356)
1kaeA L-histidinol dehydrogenase (hisd) structure complexed with l- histidinol (substrate), zinc and NAD (cofactor) (see paper)
49% identity, 99% coverage: 6:429/429 of query aligns to 10:433/434 of 1kaeA
- active site: Q259 (= Q255), H262 (= H258), E326 (= E322), H327 (= H323), D360 (= D356), H419 (= H415)
- binding L-histidinol: H262 (= H258), H327 (= H323), D360 (= D356), Y361 (= Y357), H367 (= H363)
- binding nicotinamide-adenine-dinucleotide: F58 (≠ Y52), Y130 (= Y124), P132 (= P126), P162 (= P156), G186 (= G184), P209 (= P207), G210 (= G208), N211 (= N209), F213 (≠ Y211), H262 (= H258)
- binding zinc ion: Q259 (= Q255), H262 (= H258), D360 (= D356)
P06988 Histidinol dehydrogenase; HDH; EC 1.1.1.23 from Escherichia coli (strain K12) (see 2 papers)
49% identity, 99% coverage: 6:429/429 of query aligns to 10:433/434 of P06988
- Y130 (= Y124) binding
- Q188 (= Q186) binding
- N211 (= N209) binding
- Q259 (= Q255) binding
- H262 (= H258) binding
- D360 (= D356) binding
- H419 (= H415) 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)
49% identity, 99% coverage: 6:429/429 of query aligns to 7:430/431 of 1karA
- active site: Q256 (= Q255), H259 (= H258), E323 (= E322), H324 (= H323), D357 (= D356), H416 (= H415)
- binding histamine: S137 (= S134), H259 (= H258), D357 (= D356), Y358 (= Y357), H364 (= H363)
- binding zinc ion: H259 (= H258), D357 (= D356)
1kahA L-histidinol dehydrogenase (hisd) structure complexed with l-histidine (product), zn and NAD (cofactor) (see paper)
49% identity, 99% coverage: 6:429/429 of query aligns to 7:430/431 of 1kahA
- active site: Q256 (= Q255), H259 (= H258), E323 (= E322), H324 (= H323), D357 (= D356), H416 (= H415)
- binding histidine: L135 (= L132), H259 (= H258), H324 (= H323), D357 (= D356), Y358 (= Y357), H364 (= H363), E411 (= E410), L413 (= L412), H416 (= H415)
- binding zinc ion: H259 (= H258), D357 (= D356)
P10370 Histidinol dehydrogenase; HDH; EC 1.1.1.23 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
50% identity, 99% coverage: 6:429/429 of query aligns to 10:433/434 of P10370
- H99 (= H93) mutation to N: Slight decrease in activity.
- C117 (= C111) mutation C->A,S: Almost no change in activity.
- C154 (= C148) mutation C->A,S: Almost no change in activity.
- H262 (= H258) mutation to N: 7000-fold decrease in activity.
- H327 (= H323) mutation to N: 500-fold decrease in activity.
- H367 (= H363) mutation to N: Slight decrease in activity.
- H419 (= H415) 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)
50% identity, 99% coverage: 4:429/429 of query aligns to 6:432/434 of 5vlbA
5vldF Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidine and NAD+ (see paper)
50% identity, 99% coverage: 4:429/429 of query aligns to 7:433/435 of 5vldF
- active site: Q258 (= Q255), H261 (= H258), E326 (= E322), H327 (= H323), D360 (= D356), H419 (= H415)
- binding histidine: S135 (= S134), S236 (= S233), Q258 (= Q255), H261 (= H258), E326 (= E322), H327 (= H323), D360 (= D356), Y361 (= Y357), H367 (= H363), E414 (= E410), H419 (= H415)
- binding nicotinamide-adenine-dinucleotide: F55 (≠ Y52), D56 (= D53), Y125 (= Y124), P127 (= P126), G129 (= G128), T130 (= T129), Q187 (= Q186), P208 (= P207), G209 (= G208), N210 (= N209), Y212 (= Y211), A233 (= A230), G234 (= G231), S236 (= S233), H261 (= H258), E326 (= E322), H367 (= H363), V368 (≠ T364), L369 (= L365)
- binding zinc ion: Q258 (= Q255), H261 (= H258), D360 (= D356)
5vlcA Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidinol (see paper)
51% identity, 99% coverage: 4:429/429 of query aligns to 7:430/431 of 5vlcA
- active site: Q255 (= Q255), H258 (= H258), E323 (= E322), H324 (= H323), D357 (= D356), H416 (= H415)
- binding L-histidinol: H258 (= H258), E323 (= E322), H324 (= H323), D357 (= D356), Y358 (= Y357), H364 (= H363), E411 (= E410), H416 (= H415)
- binding zinc ion: Q255 (= Q255), H258 (= H258), D357 (= D356)
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: 24:427/429 of query aligns to 22:426/432 of 4g09A
- active site: Q253 (= Q255), H256 (= H258), E321 (= E322), H322 (= H323), D355 (= D356), H414 (= H415)
- binding (3S)-3-amino-1-[4-(benzyloxy)phenyl]-4-(1H-imidazol-4-yl)butan-2-one: P126 (= P126), A130 (= A130), Y132 (≠ L132), S134 (= S134), H256 (= H258), E321 (= E322), H322 (= H323), D355 (= D356), Y356 (= Y357), H362 (= H363)
- binding zinc ion: H256 (= H258), D307 (≠ N308), D310 (≠ K311), D355 (= D356)
Query Sequence
>Echvi_2459 FitnessBrowser__Cola:Echvi_2459
MRTITNPTQSEWQKELARPVQKMKDIQKIVKPIMRKVSRQGDKALKKFALEYDHVEIDNL
LVSRDEINEAYEQVDESLKSAIQQAKVNIEKFHKAQQTEDLSMEVMEGVTCMRRSVPIQK
VGLYIPGGTAPLFSTVLMLGIPANIAGCEEIVLCTPPNKEGKIHPAILYTANLIGIDKIV
KAGGAQAIAALTYGTESVPQVAKIFGPGNQYVTAAKQLATKKGIAIDMPAGPSEVLVYAD
ESAVPAFVAADLLSQAEHGIDSQVILVATASKVAKKTLKEVDKQLAKLPRKDIAKKALEN
SIAVVMGNQEKAIALINDYAPEHLIINVANEDEVVANIVNAGSVFIGNFTPESAGDYASG
TNHTLPTYGFARNYSGVSLDSFVKKITYQKITEKGLQNLGPTIEVMAGNELLDAHKNAVS
IRLKYLKEK
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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