SitesBLAST
Comparing 5209745 FitnessBrowser__PV4:5209745 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)
58% identity, 99% coverage: 1:438/443 of query aligns to 1:430/434 of 1kaeA
- active site: Q259 (= Q267), H262 (= H270), E326 (= E334), H327 (= H335), D360 (= D368), H419 (= H427)
- binding L-histidinol: H262 (= H270), H327 (= H335), D360 (= D368), Y361 (= Y369), H367 (= H375)
- binding nicotinamide-adenine-dinucleotide: F58 (= F65), Y130 (= Y137), P132 (= P139), P162 (= P169), G186 (= G193), P209 (= P216), G210 (= G217), N211 (= N218), F213 (≠ Y220), H262 (= H270)
- binding zinc ion: Q259 (= Q267), H262 (= H270), D360 (= D368)
P06988 Histidinol dehydrogenase; HDH; EC 1.1.1.23 from Escherichia coli (strain K12) (see 2 papers)
58% identity, 99% coverage: 1:438/443 of query aligns to 1:430/434 of P06988
- M1 (= M1) modified: Initiator methionine, Removed
- Y130 (= Y137) binding
- Q188 (= Q195) binding
- N211 (= N218) binding
- Q259 (= Q267) binding
- H262 (= H270) binding
- D360 (= D368) binding
- H419 (= H427) binding
1karA L-histidinol dehydrogenase (hisd) structure complexed with histamine (inhibitor), zinc and NAD (cofactor) (see paper)
59% identity, 96% coverage: 14:438/443 of query aligns to 4:427/431 of 1karA
- active site: Q256 (= Q267), H259 (= H270), E323 (= E334), H324 (= H335), D357 (= D368), H416 (= H427)
- binding histamine: S137 (= S147), H259 (= H270), D357 (= D368), Y358 (= Y369), H364 (= H375)
- binding zinc ion: H259 (= H270), D357 (= D368)
1kahA L-histidinol dehydrogenase (hisd) structure complexed with l-histidine (product), zn and NAD (cofactor) (see paper)
59% identity, 96% coverage: 14:438/443 of query aligns to 4:427/431 of 1kahA
- active site: Q256 (= Q267), H259 (= H270), E323 (= E334), H324 (= H335), D357 (= D368), H416 (= H427)
- binding histidine: L135 (= L145), H259 (= H270), H324 (= H335), D357 (= D368), Y358 (= Y369), H364 (= H375), E411 (= E422), L413 (= L424), H416 (= H427)
- binding zinc ion: H259 (= H270), D357 (= D368)
P10370 Histidinol dehydrogenase; HDH; EC 1.1.1.23 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
57% identity, 99% coverage: 1:438/443 of query aligns to 1:430/434 of P10370
- M1 (= M1) modified: Initiator methionine, Removed
- H99 (= H106) mutation to N: Slight decrease in activity.
- C117 (= C124) mutation C->A,S: Almost no change in activity.
- C154 (= C161) mutation C->A,S: Almost no change in activity.
- H262 (= H270) mutation to N: 7000-fold decrease in activity.
- H327 (= H335) mutation to N: 500-fold decrease in activity.
- H367 (= H375) mutation to N: Slight decrease in activity.
- H419 (= H427) mutation to Q: 20-fold decrease in activity.
5vldF Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidine and NAD+ (see paper)
50% identity, 92% coverage: 27:435/443 of query aligns to 17:427/435 of 5vldF
- active site: Q258 (= Q267), H261 (= H270), E326 (= E334), H327 (= H335), D360 (= D368), H419 (= H427)
- binding histidine: S135 (= S147), S236 (= S245), Q258 (= Q267), H261 (= H270), E326 (= E334), H327 (= H335), D360 (= D368), Y361 (= Y369), H367 (= H375), E414 (= E422), H419 (= H427)
- binding nicotinamide-adenine-dinucleotide: F55 (= F65), D56 (= D66), Y125 (= Y137), P127 (= P139), G129 (= G141), T130 (≠ S142), Q187 (= Q195), P208 (= P216), G209 (= G217), N210 (= N218), Y212 (= Y220), A233 (= A242), G234 (= G243), S236 (= S245), H261 (= H270), E326 (= E334), H367 (= H375), V368 (= V376), L369 (= L377)
- binding zinc ion: Q258 (= Q267), H261 (= H270), D360 (= D368)
5vlbA Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with imidazole (see paper)
50% identity, 92% coverage: 27:435/443 of query aligns to 16:426/434 of 5vlbA
5vlcA Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidinol (see paper)
52% identity, 89% coverage: 43:435/443 of query aligns to 30:424/431 of 5vlcA
- active site: Q255 (= Q267), H258 (= H270), E323 (= E334), H324 (= H335), D357 (= D368), H416 (= H427)
- binding L-histidinol: H258 (= H270), E323 (= E334), H324 (= H335), D357 (= D368), Y358 (= Y369), H364 (= H375), E411 (= E422), H416 (= H427)
- binding zinc ion: Q255 (= Q267), H258 (= H270), D357 (= D368)
6an0A Crystal structure of histidinol dehydrogenase from elizabethkingia anophelis
47% identity, 93% coverage: 28:439/443 of query aligns to 20:432/433 of 6an0A
- active site: Q260 (= Q267), H263 (= H270), E327 (= E334), H328 (= H335), D361 (= D368), H420 (= H427)
- binding histidine: E103 (≠ F111), N104 (≠ K112), K105 (≠ G113), R118 (≠ L126), E119 (≠ R127), A120 (≠ S128), K390 (≠ R397)
- binding zinc ion: H263 (= H270), D361 (= D368)
4g09A The crystal structure of the c366s mutant of hdh from brucella suis in complex with a substituted benzyl ketone (see paper)
43% identity, 91% coverage: 38:438/443 of query aligns to 23:425/432 of 4g09A
- active site: Q253 (= Q267), H256 (= H270), E321 (= E334), H322 (= H335), D355 (= D368), H414 (= H427)
- binding (3S)-3-amino-1-[4-(benzyloxy)phenyl]-4-(1H-imidazol-4-yl)butan-2-one: P126 (= P139), A130 (= A143), Y132 (≠ L145), S134 (= S147), H256 (= H270), E321 (= E334), H322 (= H335), D355 (= D368), Y356 (= Y369), H362 (= H375)
- binding zinc ion: H256 (= H270), D307 (= D320), D310 (≠ Q323), D355 (= D368)
Query Sequence
>5209745 FitnessBrowser__PV4:5209745
MTTNTMTSTQMQRLDWQALNDQARREALSRSPLIGDANLEQQVKAIIDQVASQGDVALKA
FSQKFDKVELDALRLSDAAIAAASERVTPEIKAAIEQAKQNIETFHQAQAFKGIDLETQA
GVRCELRSEPIEKVGLYIPGGSAPLISTVLMLALPAKIAGCEQRVLVSPPPIDDAIVYAA
KACGITDIYQIGGAQAIAALAQGTESVPAVDKIFGPGNRYVTEAKRLVAQDSRCVVSIDM
PAGPSEVLVIADNEANPDFIAADLLSQAEHGPDSQVMLVTDSQTLADAVNQSLGEQLARL
PRAEIAMQALSASRTLIVEDMAQAAEVSNRYGPEHLIIQTRAPRKLLSKIRAAGSVFLGA
YTPESVGDYASGTNHVLPTYGYSRAVSSLSLADFSRRFTVQELSAEGLRGLGECVMTLAS
AEQLDAHRNAVAVRLATLTGEEK
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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