SitesBLAST
Comparing WP_057506748.1 NCBI__GCF_001431535.1:WP_057506748.1 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)
52% identity, 99% coverage: 4:430/431 of query aligns to 7:430/434 of 1kaeA
- active site: Q259 (= Q259), H262 (= H262), E326 (= E326), H327 (= H327), D360 (= D360), H419 (= H419)
- binding L-histidinol: H262 (= H262), H327 (= H327), D360 (= D360), Y361 (= Y361), H367 (= H367)
- binding nicotinamide-adenine-dinucleotide: F58 (= F55), Y130 (= Y127), P132 (= P129), P162 (= P159), G186 (= G187), P209 (= P210), G210 (= G211), N211 (= N212), F213 (= F214), H262 (= H262)
- binding zinc ion: Q259 (= Q259), H262 (= H262), D360 (= D360)
P06988 Histidinol dehydrogenase; HDH; EC 1.1.1.23 from Escherichia coli (strain K12) (see 2 papers)
52% identity, 99% coverage: 4:430/431 of query aligns to 7:430/434 of P06988
- Y130 (= Y127) binding
- Q188 (= Q189) binding
- N211 (= N212) binding
- Q259 (= Q259) binding
- H262 (= H262) binding
- D360 (= D360) binding
- H419 (= H419) 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)
52% identity, 99% coverage: 4:430/431 of query aligns to 4:427/431 of 1karA
- active site: Q256 (= Q259), H259 (= H262), E323 (= E326), H324 (= H327), D357 (= D360), H416 (= H419)
- binding histamine: S137 (= S137), H259 (= H262), D357 (= D360), Y358 (= Y361), H364 (= H367)
- binding zinc ion: H259 (= H262), D357 (= D360)
1kahA L-histidinol dehydrogenase (hisd) structure complexed with l-histidine (product), zn and NAD (cofactor) (see paper)
52% identity, 99% coverage: 4:430/431 of query aligns to 4:427/431 of 1kahA
- active site: Q256 (= Q259), H259 (= H262), E323 (= E326), H324 (= H327), D357 (= D360), H416 (= H419)
- binding histidine: L135 (= L135), H259 (= H262), H324 (= H327), D357 (= D360), Y358 (= Y361), H364 (= H367), E411 (= E414), L413 (= L416), H416 (= H419)
- binding zinc ion: H259 (= H262), D357 (= D360)
6an0A Crystal structure of histidinol dehydrogenase from elizabethkingia anophelis
49% identity, 96% coverage: 18:430/431 of query aligns to 21:431/433 of 6an0A
- active site: Q260 (= Q259), H263 (= H262), E327 (= E326), H328 (= H327), D361 (= D360), H420 (= H419)
- binding histidine: E103 (≠ S101), N104 (≠ Q102), K105 (≠ G103), R118 (= R116), E119 (≠ M117), A120 (≠ I118), K390 (≠ T389)
- binding zinc ion: H263 (= H262), D361 (= D360)
P10370 Histidinol dehydrogenase; HDH; EC 1.1.1.23 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
51% identity, 99% coverage: 4:430/431 of query aligns to 7:430/434 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 (= H262) mutation to N: 7000-fold decrease in activity.
- H327 (= H327) mutation to N: 500-fold decrease in activity.
- H367 (= H367) mutation to N: Slight decrease in activity.
- H419 (= H419) mutation to Q: 20-fold decrease in activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5vlcA Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidinol (see paper)
48% identity, 92% coverage: 33:430/431 of query aligns to 30:427/431 of 5vlcA
- active site: Q255 (= Q259), H258 (= H262), E323 (= E326), H324 (= H327), D357 (= D360), H416 (= H419)
- binding L-histidinol: H258 (= H262), E323 (= E326), H324 (= H327), D357 (= D360), Y358 (= Y361), H364 (= H367), E411 (= E414), H416 (= H419)
- binding zinc ion: Q255 (= Q259), H258 (= H262), D357 (= D360)
5vlbA Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with imidazole (see paper)
48% identity, 92% coverage: 33:430/431 of query aligns to 32:429/434 of 5vlbA
5vldF Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidine and NAD+ (see paper)
48% identity, 92% coverage: 33:430/431 of query aligns to 33:430/435 of 5vldF
- active site: Q258 (= Q259), H261 (= H262), E326 (= E326), H327 (= H327), D360 (= D360), H419 (= H419)
- binding histidine: S135 (= S137), S236 (= S237), Q258 (= Q259), H261 (= H262), E326 (= E326), H327 (= H327), D360 (= D360), Y361 (= Y361), H367 (= H367), E414 (= E414), H419 (= H419)
- binding nicotinamide-adenine-dinucleotide: F55 (= F55), D56 (= D56), Y125 (= Y127), P127 (= P129), G129 (= G131), T130 (≠ S132), Q187 (= Q189), P208 (= P210), G209 (= G211), N210 (= N212), Y212 (≠ F214), A233 (= A234), G234 (= G235), S236 (= S237), H261 (= H262), E326 (= E326), H367 (= H367), V368 (= V368), L369 (= L369)
- binding zinc ion: Q258 (= Q259), H261 (= H262), D360 (= D360)
4g09A The crystal structure of the c366s mutant of hdh from brucella suis in complex with a substituted benzyl ketone (see paper)
44% identity, 92% coverage: 32:428/431 of query aligns to 27:423/432 of 4g09A
- active site: Q253 (= Q259), H256 (= H262), E321 (= E326), H322 (= H327), D355 (= D360), H414 (= H419)
- 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 (= H262), E321 (= E326), H322 (= H327), D355 (= D360), Y356 (= Y361), H362 (= H367)
- binding zinc ion: H256 (= H262), D307 (≠ R312), D310 (= D315), D355 (= D360)
Query Sequence
>WP_057506748.1 NCBI__GCF_001431535.1:WP_057506748.1
MNRLNWSELNELDRAEALQRPVQAVAAQTRHAVAALIAQVRADGDAALREITARFDRVQL
DDIEVTAAEFEAAEQAVAVDLRAAMEEAAARIRRFHEAGMSQGYAVETAPGVHCERMIRP
IGRVGLYVPAGSAPLPSTALMLGVPAALAGCPQVVLCTPPRADGSADPAVLVAARLTGVQ
RVFKLGGAQAIAAMAHGTASVPACDKLFGPGNSFVTEAKQQVAQDGSVAIDMPAGPSEVL
VIADAGANAAFVAADLLSQAEHGPDSQVLLLTDDAALLEAVEAEVERQVALLPRETIARR
ALGASRLILVDRLQDAFEISNRYAPEHLILALREPRAWLGQVQAAGSVFLGDYTPEALGD
YCSGTNHVLPTAGAARAWSGVSVASFQNTISVQSASAEGIVAIGGCARILASAEGLDAHE
RAVALRMEAVA
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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