SitesBLAST
Comparing WP_011764552.1 NCBI__GCF_000061505.1:WP_011764552.1 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)
51% identity, 99% coverage: 5:436/436 of query aligns to 2:424/432 of 4g09A
- active site: Q253 (= Q265), H256 (= H268), E321 (= E333), H322 (= H334), D355 (= D367), H414 (= H426)
- binding (3S)-3-amino-1-[4-(benzyloxy)phenyl]-4-(1H-imidazol-4-yl)butan-2-one: P126 (= P138), A130 (= A142), Y132 (= Y144), S134 (= S146), H256 (= H268), E321 (= E333), H322 (= H334), D355 (= D367), Y356 (= Y368), H362 (= H374)
- binding zinc ion: H256 (= H268), D307 (≠ S319), D310 (≠ Q322), D355 (= D367)
1kaeA L-histidinol dehydrogenase (hisd) structure complexed with l- histidinol (substrate), zinc and NAD (cofactor) (see paper)
41% identity, 93% coverage: 31:435/436 of query aligns to 28:428/434 of 1kaeA
- active site: Q259 (= Q265), H262 (= H268), E326 (= E333), H327 (= H334), D360 (= D367), H419 (= H426)
- binding L-histidinol: H262 (= H268), H327 (= H334), D360 (= D367), Y361 (= Y368), H367 (= H374)
- binding nicotinamide-adenine-dinucleotide: F58 (= F61), Y130 (= Y136), P132 (= P138), P162 (= P168), G186 (= G195), P209 (= P218), G210 (= G219), N211 (= N220), F213 (= F222), H262 (= H268)
- binding zinc ion: Q259 (= Q265), H262 (= H268), D360 (= D367)
P06988 Histidinol dehydrogenase; HDH; EC 1.1.1.23 from Escherichia coli (strain K12) (see 2 papers)
41% identity, 93% coverage: 31:435/436 of query aligns to 28:428/434 of P06988
- Y130 (= Y136) binding NAD(+)
- Q188 (= Q197) binding NAD(+)
- N211 (= N220) binding NAD(+)
- Q259 (= Q265) binding Zn(2+)
- H262 (= H268) binding Zn(2+)
- D360 (= D367) binding Zn(2+)
- H419 (= H426) binding Zn(2+)
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)
41% identity, 93% coverage: 31:435/436 of query aligns to 28:428/434 of P10370
- H99 (= H105) mutation to N: Slight decrease in activity.
- C117 (≠ L123) mutation C->A,S: Almost no change in activity.
- C154 (≠ V160) mutation C->A,S: Almost no change in activity.
- H262 (= H268) mutation to N: 7000-fold decrease in activity.
- H327 (= H334) mutation to N: 500-fold decrease in activity.
- H367 (= H374) mutation to N: Slight decrease in activity.
- H419 (= H426) mutation to Q: 20-fold decrease in activity.
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)
41% identity, 93% coverage: 31:435/436 of query aligns to 25:425/431 of 1karA
- active site: Q256 (= Q265), H259 (= H268), E323 (= E333), H324 (= H334), D357 (= D367), H416 (= H426)
- binding histamine: S137 (= S146), H259 (= H268), D357 (= D367), Y358 (= Y368), H364 (= H374)
- binding zinc ion: H259 (= H268), D357 (= D367)
1kahA L-histidinol dehydrogenase (hisd) structure complexed with l-histidine (product), zn and NAD (cofactor) (see paper)
41% identity, 93% coverage: 31:435/436 of query aligns to 25:425/431 of 1kahA
- active site: Q256 (= Q265), H259 (= H268), E323 (= E333), H324 (= H334), D357 (= D367), H416 (= H426)
- binding histidine: L135 (≠ Y144), H259 (= H268), H324 (= H334), D357 (= D367), Y358 (= Y368), H364 (= H374), E411 (= E421), L413 (= L423), H416 (= H426)
- binding zinc ion: H259 (= H268), D357 (= D367)
5vlcA Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidinol (see paper)
36% identity, 95% coverage: 20:435/436 of query aligns to 11:425/431 of 5vlcA
- active site: Q255 (= Q265), H258 (= H268), E323 (= E333), H324 (= H334), D357 (= D367), H416 (= H426)
- binding L-histidinol: H258 (= H268), E323 (= E333), H324 (= H334), D357 (= D367), Y358 (= Y368), H364 (= H374), E411 (= E421), H416 (= H426)
- binding zinc ion: Q255 (= Q265), H258 (= H268), D357 (= D367)
6an0A Crystal structure of histidinol dehydrogenase from elizabethkingia anophelis
35% identity, 92% coverage: 33:435/436 of query aligns to 29:429/433 of 6an0A
- active site: Q260 (= Q265), H263 (= H268), E327 (= E333), H328 (= H334), D361 (= D367), H420 (= H426)
- binding histidine: E103 (= E111), N104 (≠ S112), K105 (≠ W113), R118 (≠ Q125), E119 (≠ K126), A120 (≠ V127), K390 (≠ R396)
- binding zinc ion: H263 (= H268), D361 (= D367)
5vldF Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidine and NAD+ (see paper)
37% identity, 95% coverage: 20:435/436 of query aligns to 11:428/435 of 5vldF
- active site: Q258 (= Q265), H261 (= H268), E326 (= E333), H327 (= H334), D360 (= D367), H419 (= H426)
- binding histidine: S135 (= S146), S236 (= S243), Q258 (= Q265), H261 (= H268), E326 (= E333), H327 (= H334), D360 (= D367), Y361 (= Y368), H367 (= H374), E414 (= E421), H419 (= H426)
- binding nicotinamide-adenine-dinucleotide: F55 (= F61), D56 (= D62), Y125 (= Y136), P127 (= P138), G129 (= G140), T130 (≠ R141), Q187 (= Q197), P208 (= P218), G209 (= G219), N210 (= N220), Y212 (≠ F222), A233 (= A240), G234 (= G241), S236 (= S243), H261 (= H268), E326 (= E333), H367 (= H374), V368 (= V375), L369 (= L376)
- binding zinc ion: Q258 (= Q265), H261 (= H268), D360 (= D367)
5vlbA Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with imidazole (see paper)
37% identity, 95% coverage: 20:435/436 of query aligns to 10:427/434 of 5vlbA
Query Sequence
>WP_011764552.1 NCBI__GCF_000061505.1:WP_011764552.1
MSFATPIRRLDARQPDFLATLDALLAFESEADERIDSAVTEILRAVRSTGDAAVMEYTRR
FDHVEAKSMVELELPKAELQAALDSLTVEQREALRIAADRVRIYHERQRAESWDYVEADG
SRLGQKVTPLDRVGLYVPGGRASYPSSVLMNAIPAKVAGVEELIMVVPTPRGEKNPLVLA
AAAITGVDRVFTIGGAQAVAALAYGTQTIPQVDKIVGPGNAFVAEAKRRVFGTVGIDMVA
GPSEVLIISDGSGHADWVAMDLFAQAEHDELAQSILLCTDAGFLDAVHAAIDRLLPTMPR
RETIARSLANRGALIHVGSLEQACAIANRIAPEHLELSMEDAERWIDAIRHAGAIFVGHW
AVEALGDYCAGPNHVLPTMRSARFSSPLGVYDFQKRTSIVQISEAGAQHLGKIASVLAHG
EGLQAHARSAEMRLKV
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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