SitesBLAST
Comparing WP_012853226.1 NCBI__GCF_000024385.1:WP_012853226.1 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)
4g09A The crystal structure of the c366s mutant of hdh from brucella suis in complex with a substituted benzyl ketone (see paper)
42% identity, 91% coverage: 33:430/435 of query aligns to 28:423/432 of 4g09A
- active site: Q253 (= Q259), H256 (= H262), E321 (= E328), H322 (= H329), D355 (= D362), H414 (= H421)
- binding (3S)-3-amino-1-[4-(benzyloxy)phenyl]-4-(1H-imidazol-4-yl)butan-2-one: P126 (= P129), A130 (= A133), Y132 (= Y135), S134 (= S137), H256 (= H262), E321 (= E328), H322 (= H329), D355 (= D362), Y356 (= Y363), H362 (= H369)
- binding zinc ion: H256 (= H262), D307 (= D314), D310 (≠ A317), D355 (= D362)
P10370 Histidinol dehydrogenase; HDH; EC 1.1.1.23 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
36% identity, 98% coverage: 5:430/435 of query aligns to 7:428/434 of P10370
- H99 (= H96) mutation to N: Slight decrease in activity.
- C117 (≠ V114) mutation C->A,S: Almost no change in activity.
- C154 (≠ V151) mutation C->A,S: Almost no change in activity.
- H262 (= H262) mutation to N: 7000-fold decrease in activity.
- H327 (= H329) mutation to N: 500-fold decrease in activity.
- H367 (= H369) mutation to N: Slight decrease in activity.
- H419 (= H421) 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)
36% identity, 96% coverage: 14:430/435 of query aligns to 13:427/434 of 5vlbA
5vldF Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidine and NAD+ (see paper)
36% identity, 96% coverage: 14:430/435 of query aligns to 14:428/435 of 5vldF
- active site: Q258 (= Q259), H261 (= H262), E326 (= E328), H327 (= H329), D360 (= D362), H419 (= H421)
- binding histidine: S135 (= S137), S236 (≠ T237), Q258 (= Q259), H261 (= H262), E326 (= E328), H327 (= H329), D360 (= D362), Y361 (= Y363), H367 (= H369), E414 (= E416), H419 (= H421)
- binding nicotinamide-adenine-dinucleotide: F55 (= F55), D56 (= D56), Y125 (= Y127), P127 (= P129), G129 (= G131), T130 (≠ R132), Q187 (= Q191), P208 (= P212), G209 (= G213), N210 (= N214), Y212 (≠ W216), A233 (= A234), G234 (= G235), S236 (≠ T237), H261 (= H262), E326 (= E328), H367 (= H369), V368 (= V370), L369 (= L371)
- binding zinc ion: Q258 (= Q259), H261 (= H262), D360 (= D362)
1kaeA L-histidinol dehydrogenase (hisd) structure complexed with l- histidinol (substrate), zinc and NAD (cofactor) (see paper)
35% identity, 98% coverage: 5:430/435 of query aligns to 7:428/434 of 1kaeA
- active site: Q259 (= Q259), H262 (= H262), E326 (= E328), H327 (= H329), D360 (= D362), H419 (= H421)
- binding L-histidinol: H262 (= H262), H327 (= H329), D360 (= D362), Y361 (= Y363), H367 (= H369)
- binding nicotinamide-adenine-dinucleotide: F58 (= F55), Y130 (= Y127), P132 (= P129), P162 (= P159), G186 (= G189), P209 (= P212), G210 (= G213), N211 (= N214), F213 (≠ W216), H262 (= H262)
- binding zinc ion: Q259 (= Q259), H262 (= H262), D360 (= D362)
P06988 Histidinol dehydrogenase; HDH; EC 1.1.1.23 from Escherichia coli (strain K12) (see 2 papers)
35% identity, 98% coverage: 5:430/435 of query aligns to 7:428/434 of P06988
- Y130 (= Y127) binding
- Q188 (= Q191) binding
- N211 (= N214) binding
- Q259 (= Q259) binding
- H262 (= H262) binding
- D360 (= D362) binding
- H419 (= H421) 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)
35% identity, 98% coverage: 5:430/435 of query aligns to 4:425/431 of 1karA
- active site: Q256 (= Q259), H259 (= H262), E323 (= E328), H324 (= H329), D357 (= D362), H416 (= H421)
- binding histamine: S137 (= S137), H259 (= H262), D357 (= D362), Y358 (= Y363), H364 (= H369)
- binding zinc ion: H259 (= H262), D357 (= D362)
1kahA L-histidinol dehydrogenase (hisd) structure complexed with l-histidine (product), zn and NAD (cofactor) (see paper)
35% identity, 98% coverage: 5:430/435 of query aligns to 4:425/431 of 1kahA
- active site: Q256 (= Q259), H259 (= H262), E323 (= E328), H324 (= H329), D357 (= D362), H416 (= H421)
- binding histidine: L135 (≠ Y135), H259 (= H262), H324 (= H329), D357 (= D362), Y358 (= Y363), H364 (= H369), E411 (= E416), L413 (= L418), H416 (= H421)
- binding zinc ion: H259 (= H262), D357 (= D362)
6an0A Crystal structure of histidinol dehydrogenase from elizabethkingia anophelis
34% identity, 91% coverage: 33:429/435 of query aligns to 35:428/433 of 6an0A
- active site: Q260 (= Q259), H263 (= H262), E327 (= E328), H328 (= H329), D361 (= D362), H420 (= H421)
- binding histidine: E103 (≠ R101), N104 (≠ T102), K105 (≠ D103), R118 (≠ E116), E119 (≠ R117), A120 (≠ W118), K390 (≠ G391)
- binding zinc ion: H263 (= H262), D361 (= D362)
5vlcA Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidinol (see paper)
37% identity, 93% coverage: 28:430/435 of query aligns to 25:425/431 of 5vlcA
- active site: Q255 (= Q259), H258 (= H262), E323 (= E328), H324 (= H329), D357 (= D362), H416 (= H421)
- binding L-histidinol: H258 (= H262), E323 (= E328), H324 (= H329), D357 (= D362), Y358 (= Y363), H364 (= H369), E411 (= E416), H416 (= H421)
- binding zinc ion: Q255 (= Q259), H258 (= H262), D357 (= D362)
Query Sequence
>WP_012853226.1 NCBI__GCF_000024385.1:WP_012853226.1
MISRIDLRGSLPGDLRSVLPRAELDVEAALERVRPICEDVRHRGAAAVREYTKKFDGVEL
ESLRVPAAALERALAGLDPAVRDALEESIRRARLVHRDQRRTDVTTQVVPGGTVTERWIP
VERVGLYVPGGRAVYPSSVVMNVVPAQEAGVGSLAVTSPPQQEFGGLPHPAILAACALLG
VEEVYAAGGAQSIAMLAYGTDECRPVNLVTGPGNIWVAAAKRHLRGVVGIDSEAGPTEIA
ILADASADPVHVAADLISQAEHDTLAAAVLVTDSEELAERVERELAEQVARTKHTERITQ
ALAGRQSGIVLVDDIEAGLAVVNAYAAEHLEIQTANARQVAERVRNAGAIFIGPHSPVSL
GDYLAGSNHVLPTGGCACHSSGLSVQSFLRGVHVVEYDRAALAEATARVVALAEAEDLPA
HGAAMKARFNWEIPT
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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