SitesBLAST
Comparing WP_019895889.1 NCBI__GCF_000384235.1:WP_019895889.1 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)
4g09A The crystal structure of the c366s mutant of hdh from brucella suis in complex with a substituted benzyl ketone (see paper)
49% identity, 99% coverage: 4:432/432 of query aligns to 1:423/432 of 4g09A
- active site: Q253 (= Q262), H256 (= H265), E321 (= E330), H322 (= H331), D355 (= D364), H414 (= H423)
- binding (3S)-3-amino-1-[4-(benzyloxy)phenyl]-4-(1H-imidazol-4-yl)butan-2-one: P126 (= P135), A130 (= A139), Y132 (= Y141), S134 (= S143), H256 (= H265), E321 (= E330), H322 (= H331), D355 (= D364), Y356 (= Y365), H362 (= H371)
- binding zinc ion: H256 (= H265), D307 (≠ N316), D310 (≠ Q319), D355 (= D364)
1kaeA L-histidinol dehydrogenase (hisd) structure complexed with l- histidinol (substrate), zinc and NAD (cofactor) (see paper)
39% identity, 93% coverage: 31:432/432 of query aligns to 31:428/434 of 1kaeA
- active site: Q259 (= Q262), H262 (= H265), E326 (= E330), H327 (= H331), D360 (= D364), H419 (= H423)
- binding L-histidinol: H262 (= H265), H327 (= H331), D360 (= D364), Y361 (= Y365), H367 (= H371)
- binding nicotinamide-adenine-dinucleotide: F58 (= F58), Y130 (= Y133), P132 (= P135), P162 (= P165), G186 (= G192), P209 (= P215), G210 (= G216), N211 (= N217), F213 (= F219), H262 (= H265)
- binding zinc ion: Q259 (= Q262), H262 (= H265), D360 (= D364)
P06988 Histidinol dehydrogenase; HDH; EC 1.1.1.23 from Escherichia coli (strain K12) (see 2 papers)
39% identity, 93% coverage: 31:432/432 of query aligns to 31:428/434 of P06988
- Y130 (= Y133) binding NAD(+)
- Q188 (= Q194) binding NAD(+)
- N211 (= N217) binding NAD(+)
- Q259 (= Q262) binding Zn(2+)
- H262 (= H265) binding Zn(2+)
- D360 (= D364) binding Zn(2+)
- H419 (= H423) binding Zn(2+)
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)
39% identity, 93% coverage: 31:432/432 of query aligns to 28:425/431 of 1karA
- active site: Q256 (= Q262), H259 (= H265), E323 (= E330), H324 (= H331), D357 (= D364), H416 (= H423)
- binding histamine: S137 (= S143), H259 (= H265), D357 (= D364), Y358 (= Y365), H364 (= H371)
- binding zinc ion: H259 (= H265), D357 (= D364)
1kahA L-histidinol dehydrogenase (hisd) structure complexed with l-histidine (product), zn and NAD (cofactor) (see paper)
39% identity, 93% coverage: 31:432/432 of query aligns to 28:425/431 of 1kahA
- active site: Q256 (= Q262), H259 (= H265), E323 (= E330), H324 (= H331), D357 (= D364), H416 (= H423)
- binding histidine: L135 (≠ Y141), H259 (= H265), H324 (= H331), D357 (= D364), Y358 (= Y365), H364 (= H371), E411 (= E418), L413 (= L420), H416 (= H423)
- binding zinc ion: H259 (= H265), D357 (= D364)
P10370 Histidinol dehydrogenase; HDH; EC 1.1.1.23 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
38% identity, 93% coverage: 31:432/432 of query aligns to 31:428/434 of P10370
- H99 (= H102) mutation to N: Slight decrease in activity.
- C117 (≠ L120) mutation C->A,S: Almost no change in activity.
- C154 (≠ V157) mutation C->A,S: Almost no change in activity.
- H262 (= H265) mutation to N: 7000-fold decrease in activity.
- H327 (= H331) mutation to N: 500-fold decrease in activity.
- H367 (= H371) mutation to N: Slight decrease in activity.
- H419 (= H423) 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
34% identity, 93% coverage: 32:432/432 of query aligns to 31:429/433 of 6an0A
- active site: Q260 (= Q262), H263 (= H265), E327 (= E330), H328 (= H331), D361 (= D364), H420 (= H423)
- binding histidine: E103 (≠ S107), N104 (≠ E108), K105 (≠ S109), R118 (≠ Q122), E119 (≠ Q123), A120 (≠ V124), K390 (≠ R393)
- binding zinc ion: H263 (= H265), D361 (= D364)
5vldF Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidine and NAD+ (see paper)
36% identity, 97% coverage: 16:432/432 of query aligns to 13:428/435 of 5vldF
- active site: Q258 (= Q262), H261 (= H265), E326 (= E330), H327 (= H331), D360 (= D364), H419 (= H423)
- binding histidine: S135 (= S143), S236 (= S240), Q258 (= Q262), H261 (= H265), E326 (= E330), H327 (= H331), D360 (= D364), Y361 (= Y365), H367 (= H371), E414 (= E418), H419 (= H423)
- binding nicotinamide-adenine-dinucleotide: F55 (= F58), D56 (= D59), Y125 (= Y133), P127 (= P135), G129 (= G137), T130 (≠ K138), Q187 (= Q194), P208 (= P215), G209 (= G216), N210 (= N217), Y212 (≠ F219), A233 (= A237), G234 (= G238), S236 (= S240), H261 (= H265), E326 (= E330), H367 (= H371), V368 (= V372), L369 (= L373)
- binding zinc ion: Q258 (= Q262), H261 (= H265), D360 (= D364)
5vlcA Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidinol (see paper)
36% identity, 95% coverage: 21:432/432 of query aligns to 15:425/431 of 5vlcA
- active site: Q255 (= Q262), H258 (= H265), E323 (= E330), H324 (= H331), D357 (= D364), H416 (= H423)
- binding L-histidinol: H258 (= H265), E323 (= E330), H324 (= H331), D357 (= D364), Y358 (= Y365), H364 (= H371), E411 (= E418), H416 (= H423)
- binding zinc ion: Q255 (= Q262), H258 (= H265), D357 (= D364)
5vlbA Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with imidazole (see paper)
36% identity, 97% coverage: 16:432/432 of query aligns to 12:427/434 of 5vlbA
Query Sequence
>WP_019895889.1 NCBI__GCF_000384235.1:WP_019895889.1
MLKIETLFANASDFYTKLDRLLAWEGVSDTSVNEVVRGVLKAVREQGDQALLHYTEKFDR
LTLKDAAELEIPASEMHAALARIPAKQREALEFSAQRVRQYHERQVSESWSYTEADGTLL
GQQVTPLDKVGLYVPGGKAAYPSSVVMNAVPAKVAGVEQLIMVVPTPDGEVNDMVLAAAA
ICDVDRVFTLGGAQAVAALAYGTETVPPVDKIVGPGNIFVATAKREVFGTVGIDMIAGPS
EILVYCDGQTDPDWIAMDLFSQAEHDEDAQSILVTPDAEFAKQVEQSLNKLIDQMPREAI
IRKALETRGAIIVVENETQGCDVINHVAPEHLELSVADPQAMLPSIRHAGAIFMGRYTAE
ALGDYCAGPNHVLPTSRTARFSSPLGVYDFQKRSSLIMCSPEGSRMLGEYAAELADGEGL
QAHAQSARYRLK
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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