SitesBLAST
Comparing 6937801 FitnessBrowser__SB2B:6937801 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)
1kaeA L-histidinol dehydrogenase (hisd) structure complexed with l- histidinol (substrate), zinc and NAD (cofactor) (see paper)
61% identity, 98% coverage: 6:431/435 of query aligns to 9:433/434 of 1kaeA
- active site: Q259 (= Q257), H262 (= H260), E326 (= E324), H327 (= H325), D360 (= D358), H419 (= H417)
- binding L-histidinol: H262 (= H260), H327 (= H325), D360 (= D358), Y361 (= Y359), H367 (= H365)
- binding nicotinamide-adenine-dinucleotide: F58 (= F55), Y130 (= Y127), P132 (= P129), P162 (= P159), G186 (= G183), P209 (= P206), G210 (= G207), N211 (= N208), F213 (≠ Y210), H262 (= H260)
- binding zinc ion: Q259 (= Q257), H262 (= H260), D360 (= D358)
P06988 Histidinol dehydrogenase; HDH; EC 1.1.1.23 from Escherichia coli (strain K12) (see 2 papers)
61% identity, 98% coverage: 6:431/435 of query aligns to 9:433/434 of P06988
- Y130 (= Y127) binding
- Q188 (= Q185) binding
- N211 (= N208) binding
- Q259 (= Q257) binding
- H262 (= H260) binding
- D360 (= D358) binding
- H419 (= H417) 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)
61% identity, 98% coverage: 6:431/435 of query aligns to 6:430/431 of 1karA
- active site: Q256 (= Q257), H259 (= H260), E323 (= E324), H324 (= H325), D357 (= D358), H416 (= H417)
- binding histamine: S137 (= S137), H259 (= H260), D357 (= D358), Y358 (= Y359), H364 (= H365)
- binding zinc ion: H259 (= H260), D357 (= D358)
1kahA L-histidinol dehydrogenase (hisd) structure complexed with l-histidine (product), zn and NAD (cofactor) (see paper)
61% identity, 98% coverage: 6:431/435 of query aligns to 6:430/431 of 1kahA
- active site: Q256 (= Q257), H259 (= H260), E323 (= E324), H324 (= H325), D357 (= D358), H416 (= H417)
- binding histidine: L135 (= L135), H259 (= H260), H324 (= H325), D357 (= D358), Y358 (= Y359), H364 (= H365), E411 (= E412), L413 (= L414), H416 (= H417)
- binding zinc ion: H259 (= H260), D357 (= D358)
P10370 Histidinol dehydrogenase; HDH; EC 1.1.1.23 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
60% identity, 99% coverage: 1:431/435 of query aligns to 3:433/434 of P10370
- H99 (= H96) mutation to N: Slight decrease in activity.
- C117 (= C114) mutation C->A,S: Almost no change in activity.
- C154 (= C151) mutation C->A,S: Almost no change in activity.
- H262 (= H260) mutation to N: 7000-fold decrease in activity.
- H327 (= H325) mutation to N: 500-fold decrease in activity.
- H367 (= H365) mutation to N: Slight decrease in activity.
- H419 (= H417) 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
47% identity, 98% coverage: 1:428/435 of query aligns to 6:431/433 of 6an0A
- active site: Q260 (= Q257), H263 (= H260), E327 (= E324), H328 (= H325), D361 (= D358), H420 (= H417)
- binding histidine: E103 (≠ F101), N104 (≠ S102), K105 (≠ E103), R118 (≠ L116), E119 (≠ K117), A120 (≠ S118), K390 (≠ R387)
- binding zinc ion: H263 (= H260), D361 (= D358)
5vlbA Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with imidazole (see paper)
49% identity, 96% coverage: 17:435/435 of query aligns to 16:433/434 of 5vlbA
5vldF Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidine and NAD+ (see paper)
49% identity, 96% coverage: 17:435/435 of query aligns to 17:434/435 of 5vldF
- active site: Q258 (= Q257), H261 (= H260), E326 (= E324), H327 (= H325), D360 (= D358), H419 (= H417)
- binding histidine: S135 (= S137), S236 (= S235), Q258 (= Q257), H261 (= H260), E326 (= E324), H327 (= H325), D360 (= D358), Y361 (= Y359), H367 (= H365), E414 (= E412), H419 (= H417)
- binding nicotinamide-adenine-dinucleotide: F55 (= F55), D56 (= D56), Y125 (= Y127), P127 (= P129), G129 (= G131), T130 (≠ S132), Q187 (= Q185), P208 (= P206), G209 (= G207), N210 (= N208), Y212 (= Y210), A233 (= A232), G234 (= G233), S236 (= S235), H261 (= H260), E326 (= E324), H367 (= H365), V368 (= V366), L369 (= L367)
- binding zinc ion: Q258 (= Q257), H261 (= H260), D360 (= D358)
5vlcA Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidinol (see paper)
50% identity, 93% coverage: 33:435/435 of query aligns to 30:431/431 of 5vlcA
- active site: Q255 (= Q257), H258 (= H260), E323 (= E324), H324 (= H325), D357 (= D358), H416 (= H417)
- binding L-histidinol: H258 (= H260), E323 (= E324), H324 (= H325), D357 (= D358), Y358 (= Y359), H364 (= H365), E411 (= E412), H416 (= H417)
- binding zinc ion: Q255 (= Q257), H258 (= H260), D357 (= D358)
4g09A The crystal structure of the c366s mutant of hdh from brucella suis in complex with a substituted benzyl ketone (see paper)
43% identity, 93% coverage: 23:426/435 of query aligns to 19:423/432 of 4g09A
- active site: Q253 (= Q257), H256 (= H260), E321 (= E324), H322 (= H325), D355 (= D358), H414 (= H417)
- 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 (= H260), E321 (= E324), H322 (= H325), D355 (= D358), Y356 (= Y359), H362 (= H365)
- binding zinc ion: H256 (= H260), D307 (≠ T310), D310 (≠ E313), D355 (= D358)
Query Sequence
>6937801 FitnessBrowser__SB2B:6937801
METLVWNTLSEDAKRQALSRSPLVGDDSLATSVSDILCNVKRRGDSTLIEYAARFDKAEI
DTLALSADEIAAACERVSPELKDAINAARTNIARFHSAQQFSEISLETQPGVRCELKSEA
IEKVGLYIPGGSAPLISTVLMLAVPAAIAGCTKRVLVSPPPIDDAILYAASVCGITDVFQ
IGGAQAIAALAYGTESVPKVDKIFGPGNRYVTEAKAQVARDTQAAVTIDMPAGPSEVLVI
ADDAANPEFIAADLLSQAEHGSDSQVIFVTDSRTQANAVEAALERQLTLLPRRETAEGAL
SCSRIIITATLDEAAIVSNLYAPEHLIIQTREPRALLPRIRAAGSVFLGAYTPESVGDYA
SGTNHVLPTYGYSKTVSSLSLADFCRRFTVQELSAEGLKGLGQTVMTLAAAESLDAHKNA
VKVRLDAIAREENRQ
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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