SitesBLAST
Comparing 201230 FitnessBrowser__MR1:201230 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)
1karA L-histidinol dehydrogenase (hisd) structure complexed with histamine (inhibitor), zinc and NAD (cofactor) (see paper)
57% identity, 99% coverage: 3:437/438 of query aligns to 3:428/431 of 1karA
- active site: Q256 (= Q265), H259 (= H268), E323 (= E332), H324 (= H333), D357 (= D366), H416 (= H425)
- binding histamine: S137 (= S145), H259 (= H268), D357 (= D366), Y358 (= Y367), H364 (= H373)
- binding zinc ion: H259 (= H268), D357 (= D366)
1kahA L-histidinol dehydrogenase (hisd) structure complexed with l-histidine (product), zn and NAD (cofactor) (see paper)
57% identity, 99% coverage: 3:437/438 of query aligns to 3:428/431 of 1kahA
- active site: Q256 (= Q265), H259 (= H268), E323 (= E332), H324 (= H333), D357 (= D366), H416 (= H425)
- binding histidine: L135 (= L143), H259 (= H268), H324 (= H333), D357 (= D366), Y358 (= Y367), H364 (= H373), E411 (= E420), L413 (= L422), H416 (= H425)
- binding zinc ion: H259 (= H268), D357 (= D366)
1kaeA L-histidinol dehydrogenase (hisd) structure complexed with l- histidinol (substrate), zinc and NAD (cofactor) (see paper)
57% identity, 99% coverage: 3:437/438 of query aligns to 6:431/434 of 1kaeA
- active site: Q259 (= Q265), H262 (= H268), E326 (= E332), H327 (= H333), D360 (= D366), H419 (= H425)
- binding L-histidinol: H262 (= H268), H327 (= H333), D360 (= D366), Y361 (= Y367), H367 (= H373)
- binding nicotinamide-adenine-dinucleotide: F58 (= F55), Y130 (= Y135), P132 (= P137), P162 (= P167), G186 (= G191), P209 (= P214), G210 (= G215), N211 (= N216), F213 (≠ Y218), H262 (= H268)
- binding zinc ion: Q259 (= Q265), H262 (= H268), D360 (= D366)
P06988 Histidinol dehydrogenase; HDH; EC 1.1.1.23 from Escherichia coli (strain K12) (see 2 papers)
57% identity, 99% coverage: 3:437/438 of query aligns to 6:431/434 of P06988
- Y130 (= Y135) binding
- Q188 (= Q193) binding
- N211 (= N216) binding
- Q259 (= Q265) binding
- H262 (= H268) binding
- D360 (= D366) binding
- H419 (= H425) 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)
57% identity, 99% coverage: 3:437/438 of query aligns to 6:431/434 of P10370
- H99 (= H104) mutation to N: Slight decrease in activity.
- C117 (= C122) mutation C->A,S: Almost no change in activity.
- C154 (= C159) mutation C->A,S: Almost no change in activity.
- H262 (= H268) mutation to N: 7000-fold decrease in activity.
- H327 (= H333) mutation to N: 500-fold decrease in activity.
- H367 (= H373) mutation to N: Slight decrease in activity.
- H419 (= H425) 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
48% identity, 99% coverage: 3:436/438 of query aligns to 6:431/433 of 6an0A
- active site: Q260 (= Q265), H263 (= H268), E327 (= E332), H328 (= H333), D361 (= D366), H420 (= H425)
- binding histidine: E103 (≠ F109), N104 (≠ R110), K105 (≠ P111), R118 (≠ L124), E119 (≠ R125), A120 (≠ S126), K390 (≠ R395)
- binding zinc ion: H263 (= H268), D361 (= D366)
5vlbA Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with imidazole (see paper)
49% identity, 96% coverage: 17:437/438 of query aligns to 16:430/434 of 5vlbA
5vldF Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidine and NAD+ (see paper)
49% identity, 96% coverage: 17:437/438 of query aligns to 17:431/435 of 5vldF
- active site: Q258 (= Q265), H261 (= H268), E326 (= E332), H327 (= H333), D360 (= D366), H419 (= H425)
- binding histidine: S135 (= S145), S236 (= S243), Q258 (= Q265), H261 (= H268), E326 (= E332), H327 (= H333), D360 (= D366), Y361 (= Y367), H367 (= H373), E414 (= E420), H419 (= H425)
- binding nicotinamide-adenine-dinucleotide: F55 (= F55), D56 (= D56), Y125 (= Y135), P127 (= P137), G129 (= G139), T130 (≠ S140), Q187 (= Q193), P208 (= P214), G209 (= G215), N210 (= N216), Y212 (= Y218), A233 (= A240), G234 (= G241), S236 (= S243), H261 (= H268), E326 (= E332), H367 (= H373), V368 (= V374), L369 (= L375)
- binding zinc ion: Q258 (= Q265), H261 (= H268), D360 (= D366)
5vlcA Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidinol (see paper)
50% identity, 92% coverage: 33:437/438 of query aligns to 30:428/431 of 5vlcA
- active site: Q255 (= Q265), H258 (= H268), E323 (= E332), H324 (= H333), D357 (= D366), H416 (= H425)
- binding L-histidinol: H258 (= H268), E323 (= E332), H324 (= H333), D357 (= D366), Y358 (= Y367), H364 (= H373), E411 (= E420), H416 (= H425)
- binding zinc ion: Q255 (= Q265), H258 (= H268), D357 (= D366)
4g09A The crystal structure of the c366s mutant of hdh from brucella suis in complex with a substituted benzyl ketone (see paper)
44% identity, 97% coverage: 13:437/438 of query aligns to 12:426/432 of 4g09A
- active site: Q253 (= Q265), H256 (= H268), E321 (= E332), H322 (= H333), D355 (= D366), H414 (= H425)
- binding (3S)-3-amino-1-[4-(benzyloxy)phenyl]-4-(1H-imidazol-4-yl)butan-2-one: P126 (= P137), A130 (= A141), Y132 (≠ L143), S134 (= S145), H256 (= H268), E321 (= E332), H322 (= H333), D355 (= D366), Y356 (= Y367), H362 (= H373)
- binding zinc ion: H256 (= H268), D307 (= D318), D310 (≠ E321), D355 (= D366)
Query Sequence
>201230 FitnessBrowser__MR1:201230
MDMLTWAALSADEQKTALQRSPLIGDSGLEQSVRAIVDAVASRGDAAIKEFNQKFDGARL
ANISSANSDNLRLSEHEIEAASARVSPELKAAIAQAMANIDVFHSAQQFRPIDIETQAGV
RCELRSEPIEKVGLYIPGGSAPLISTVLMLALPATIAGCEQRVLVSPPPINDAIVYAANV
CGITEIYQVGGAQAIAALAFGTETIPSVDKIFGPGNRYVTEAKRLVSQDGRCTVSIDMPA
GPSEVLVIADSDANAQFIAADLLSQAEHGPDSQVILVTDSLPLAQAVNQALKSQLAALPR
QEIAATALKGSRTILVKDMQEAALVSNRYGPEHLIIQTRFPREVLNNIRAAGSVFLGAYT
PESVGDYASGTNHVLPTYGYSRAVSSLSLADFSRRFTVQELSAKGLLGLGQAVMTLASNE
LLDAHKNAVAVRLASLKG
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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