SitesBLAST
Comparing WP_011736875.1 NCBI__GCF_000015045.1:WP_011736875.1 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)
52% identity, 98% coverage: 8:429/430 of query aligns to 8:423/432 of 4g09A
- active site: Q253 (= Q259), H256 (= H262), E321 (= E327), H322 (= H328), D355 (= D361), H414 (= H420)
- binding (3S)-3-amino-1-[4-(benzyloxy)phenyl]-4-(1H-imidazol-4-yl)butan-2-one: P126 (= P132), A130 (= A136), Y132 (= Y138), S134 (= S140), H256 (= H262), E321 (= E327), H322 (= H328), D355 (= D361), Y356 (= Y362), H362 (= H368)
- binding zinc ion: H256 (= H262), D307 (≠ S313), D310 (≠ E316), D355 (= D361)
6an0A Crystal structure of histidinol dehydrogenase from elizabethkingia anophelis
40% identity, 93% coverage: 29:428/430 of query aligns to 31:428/433 of 6an0A
- active site: Q260 (= Q259), H263 (= H262), E327 (= E327), H328 (= H328), D361 (= D361), H420 (= H420)
- binding histidine: E103 (≠ Q104), N104 (≠ Q105), K105 (≠ T106), R118 (≠ Q119), E119 (≠ K120), A120 (≠ V121), K390 (= K390)
- binding zinc ion: H263 (= H262), D361 (= D361)
P10370 Histidinol dehydrogenase; HDH; EC 1.1.1.23 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
41% identity, 93% coverage: 32:429/430 of query aligns to 35:428/434 of P10370
- H99 (= H99) mutation to N: Slight decrease in activity.
- C117 (≠ L117) mutation C->A,S: Almost no change in activity.
- C154 (≠ V154) mutation C->A,S: Almost no change in activity.
- H262 (= H262) mutation to N: 7000-fold decrease in activity.
- H327 (= H328) mutation to N: 500-fold decrease in activity.
- H367 (= H368) mutation to N: Slight decrease in activity.
- H419 (= H420) 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)
39% identity, 96% coverage: 19:429/430 of query aligns to 23:425/431 of 1karA
- active site: Q256 (= Q259), H259 (= H262), E323 (= E327), H324 (= H328), D357 (= D361), H416 (= H420)
- binding histamine: S137 (= S140), H259 (= H262), D357 (= D361), Y358 (= Y362), H364 (= H368)
- binding zinc ion: H259 (= H262), D357 (= D361)
1kahA L-histidinol dehydrogenase (hisd) structure complexed with l-histidine (product), zn and NAD (cofactor) (see paper)
39% identity, 96% coverage: 19:429/430 of query aligns to 23:425/431 of 1kahA
- active site: Q256 (= Q259), H259 (= H262), E323 (= E327), H324 (= H328), D357 (= D361), H416 (= H420)
- binding histidine: L135 (≠ Y138), H259 (= H262), H324 (= H328), D357 (= D361), Y358 (= Y362), H364 (= H368), E411 (= E415), L413 (= L417), H416 (= H420)
- binding zinc ion: H259 (= H262), D357 (= D361)
1kaeA L-histidinol dehydrogenase (hisd) structure complexed with l- histidinol (substrate), zinc and NAD (cofactor) (see paper)
39% identity, 96% coverage: 19:429/430 of query aligns to 26:428/434 of 1kaeA
- active site: Q259 (= Q259), H262 (= H262), E326 (= E327), H327 (= H328), D360 (= D361), H419 (= H420)
- binding L-histidinol: H262 (= H262), H327 (= H328), D360 (= D361), Y361 (= Y362), H367 (= H368)
- binding nicotinamide-adenine-dinucleotide: F58 (= F55), Y130 (= Y130), P132 (= P132), P162 (= P162), G186 (= G189), P209 (= P212), G210 (= G213), N211 (= N214), F213 (≠ Y216), H262 (= H262)
- binding zinc ion: Q259 (= Q259), H262 (= H262), D360 (= D361)
P06988 Histidinol dehydrogenase; HDH; EC 1.1.1.23 from Escherichia coli (strain K12) (see 2 papers)
39% identity, 96% coverage: 19:429/430 of query aligns to 26:428/434 of P06988
- Y130 (= Y130) binding NAD(+)
- Q188 (= Q191) binding NAD(+)
- N211 (= N214) binding NAD(+)
- Q259 (= Q259) binding Zn(2+)
- H262 (= H262) binding Zn(2+)
- D360 (= D361) binding Zn(2+)
- H419 (= H420) binding Zn(2+)
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)
39% identity, 92% coverage: 33:428/430 of query aligns to 32:426/434 of 5vlbA
5vldF Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidine and NAD+ (see paper)
39% identity, 92% coverage: 33:428/430 of query aligns to 33:427/435 of 5vldF
- active site: Q258 (= Q259), H261 (= H262), E326 (= E327), H327 (= H328), D360 (= D361), H419 (= H420)
- binding histidine: S135 (= S140), S236 (= S237), Q258 (= Q259), H261 (= H262), E326 (= E327), H327 (= H328), D360 (= D361), Y361 (= Y362), H367 (= H368), E414 (= E415), H419 (= H420)
- binding nicotinamide-adenine-dinucleotide: F55 (= F55), D56 (= D56), Y125 (= Y130), P127 (= P132), G129 (= G134), T130 (≠ K135), Q187 (= Q191), P208 (= P212), G209 (= G213), N210 (= N214), Y212 (= Y216), A233 (= A234), G234 (= G235), S236 (= S237), H261 (= H262), E326 (= E327), H367 (= H368), V368 (≠ T369), L369 (= L370)
- binding zinc ion: Q258 (= Q259), H261 (= H262), D360 (= D361)
5vlcA Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidinol (see paper)
39% identity, 92% coverage: 33:428/430 of query aligns to 30:424/431 of 5vlcA
- active site: Q255 (= Q259), H258 (= H262), E323 (= E327), H324 (= H328), D357 (= D361), H416 (= H420)
- binding L-histidinol: H258 (= H262), E323 (= E327), H324 (= H328), D357 (= D361), Y358 (= Y362), H364 (= H368), E411 (= E415), H416 (= H420)
- binding zinc ion: Q255 (= Q259), H258 (= H262), D357 (= D361)
Query Sequence
>WP_011736875.1 NCBI__GCF_000015045.1:WP_011736875.1
MKLMDMRDTDFGERFAVILSRGEEIDRAVEGSVAEIIADVRSRGDQALLDLTRRFDRLET
SSVAELEVGETEIDAALAAVAADDLASLRHAVERVTRFHEKQRQQTWLSTEEPDIMLGQK
VTPLERVGIYVPGGKASYPSSVIMNAVPARVAGVREILMVTPTPGGEVNPHVLAAARLSG
VDRIFRIGGAQAVAALAYGTATIPRVDKITGPGNIYVATAKKLVFGQVGIDMIAGPSEIL
VINDGSGDTAHVASDLLSQAEHDELASSILITTDRSFGERVAGEVERQLGLLSRESIARA
SWESYGAIIVAGSLDEAVAFSNRIAPEHLELAVADPFSLLPAITNAGAIFMGHWTPEAAG
DYLAGPNHTLPTGGTARFFSPLSVDDFVKKSSIVCLSEGGLKRLGRDIVRIAGLEGLEAH
ARSVSIRLDR
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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