SitesBLAST
Comparing 349729 FitnessBrowser__Btheta:349729 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)
6an0A Crystal structure of histidinol dehydrogenase from elizabethkingia anophelis
56% identity, 98% coverage: 8:428/428 of query aligns to 12:432/433 of 6an0A
- active site: Q260 (= Q256), H263 (= H259), E327 (= E323), H328 (= H324), D361 (= D357), H420 (= H416)
- binding histidine: E103 (≠ F99), N104 (≠ V100), K105 (≠ G101), R118 (≠ Q114), E119 (≠ K115), A120 (= A116), K390 (= K386)
- binding zinc ion: H263 (= H259), D361 (= D357)
1kaeA L-histidinol dehydrogenase (hisd) structure complexed with l- histidinol (substrate), zinc and NAD (cofactor) (see paper)
55% identity, 98% coverage: 9:428/428 of query aligns to 13:431/434 of 1kaeA
- active site: Q259 (= Q256), H262 (= H259), E326 (= E323), H327 (= H324), D360 (= D357), H419 (= H416)
- binding L-histidinol: H262 (= H259), H327 (= H324), D360 (= D357), Y361 (= Y358), H367 (= H364)
- binding nicotinamide-adenine-dinucleotide: F58 (= F53), Y130 (= Y125), P132 (= P127), P162 (= P157), G186 (= G185), P209 (= P208), G210 (= G209), N211 (= N210), F213 (≠ Y212), H262 (= H259)
- binding zinc ion: Q259 (= Q256), H262 (= H259), D360 (= D357)
P06988 Histidinol dehydrogenase; HDH; EC 1.1.1.23 from Escherichia coli (strain K12) (see 2 papers)
55% identity, 98% coverage: 9:428/428 of query aligns to 13:431/434 of P06988
- Y130 (= Y125) binding
- Q188 (= Q187) binding
- N211 (= N210) binding
- Q259 (= Q256) binding
- H262 (= H259) binding
- D360 (= D357) binding
- H419 (= H416) 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)
55% identity, 98% coverage: 9:428/428 of query aligns to 10:428/431 of 1karA
- active site: Q256 (= Q256), H259 (= H259), E323 (= E323), H324 (= H324), D357 (= D357), H416 (= H416)
- binding histamine: S137 (= S135), H259 (= H259), D357 (= D357), Y358 (= Y358), H364 (= H364)
- binding zinc ion: H259 (= H259), D357 (= D357)
1kahA L-histidinol dehydrogenase (hisd) structure complexed with l-histidine (product), zn and NAD (cofactor) (see paper)
55% identity, 98% coverage: 9:428/428 of query aligns to 10:428/431 of 1kahA
- active site: Q256 (= Q256), H259 (= H259), E323 (= E323), H324 (= H324), D357 (= D357), H416 (= H416)
- binding histidine: L135 (= L133), H259 (= H259), H324 (= H324), D357 (= D357), Y358 (= Y358), H364 (= H364), E411 (= E411), L413 (= L413), H416 (= H416)
- binding zinc ion: H259 (= H259), D357 (= D357)
P10370 Histidinol dehydrogenase; HDH; EC 1.1.1.23 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
55% identity, 98% coverage: 9:428/428 of query aligns to 13:431/434 of P10370
- H99 (= H94) mutation to N: Slight decrease in activity.
- C117 (= C112) mutation C->A,S: Almost no change in activity.
- C154 (= C149) mutation C->A,S: Almost no change in activity.
- H262 (= H259) mutation to N: 7000-fold decrease in activity.
- H327 (= H324) mutation to N: 500-fold decrease in activity.
- H367 (= H364) mutation to N: Slight decrease in activity.
- H419 (= H416) mutation to Q: 20-fold decrease in activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5vldF Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidine and NAD+ (see paper)
52% identity, 96% coverage: 16:428/428 of query aligns to 18:431/435 of 5vldF
- active site: Q258 (= Q256), H261 (= H259), E326 (= E323), H327 (= H324), D360 (= D357), H419 (= H416)
- binding histidine: S135 (= S135), S236 (= S234), Q258 (= Q256), H261 (= H259), E326 (= E323), H327 (= H324), D360 (= D357), Y361 (= Y358), H367 (= H364), E414 (= E411), H419 (= H416)
- binding nicotinamide-adenine-dinucleotide: F55 (= F53), D56 (= D54), Y125 (= Y125), P127 (= P127), G129 (= G129), T130 (= T130), Q187 (= Q187), P208 (= P208), G209 (= G209), N210 (= N210), Y212 (= Y212), A233 (= A231), G234 (= G232), S236 (= S234), H261 (= H259), E326 (= E323), H367 (= H364), V368 (≠ T365), L369 (= L366)
- binding zinc ion: Q258 (= Q256), H261 (= H259), D360 (= D357)
5vlbA Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with imidazole (see paper)
52% identity, 96% coverage: 16:428/428 of query aligns to 17:430/434 of 5vlbA
5vlcA Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidinol (see paper)
52% identity, 96% coverage: 16:428/428 of query aligns to 18:428/431 of 5vlcA
- active site: Q255 (= Q256), H258 (= H259), E323 (= E323), H324 (= H324), D357 (= D357), H416 (= H416)
- binding L-histidinol: H258 (= H259), E323 (= E323), H324 (= H324), D357 (= D357), Y358 (= Y358), H364 (= H364), E411 (= E411), H416 (= H416)
- binding zinc ion: Q255 (= Q256), H258 (= H259), D357 (= D357)
4g09A The crystal structure of the c366s mutant of hdh from brucella suis in complex with a substituted benzyl ketone (see paper)
44% identity, 95% coverage: 22:428/428 of query aligns to 19:426/432 of 4g09A
- active site: Q253 (= Q256), H256 (= H259), E321 (= E323), H322 (= H324), D355 (= D357), H414 (= H416)
- binding (3S)-3-amino-1-[4-(benzyloxy)phenyl]-4-(1H-imidazol-4-yl)butan-2-one: P126 (= P127), A130 (= A131), Y132 (≠ L133), S134 (= S135), H256 (= H259), E321 (= E323), H322 (= H324), D355 (= D357), Y356 (= Y358), H362 (= H364)
- binding zinc ion: H256 (= H259), D307 (= D309), D310 (≠ E312), D355 (= D357)
Query Sequence
>349729 FitnessBrowser__Btheta:349729
MMKLIKYPSKEQWAELLKRPALNTESLFDTVRTIINKVRAEGDKAVLEYEAAFDKVTLSA
LTVTSEEIQKAEGLISDELKSAITLAKRNIETFHSSQRFVGKKVETMEGVTCWQKAVGIE
KVGLYIPGGTAPLFSTVLMLAVPAKIAGCREIVLCTPPDKNGNIHPAILFAAQLAGVSKI
FKAGGVQAIAAMAYGTESVPKVYKIFGPGNQYVTAAKQLVSLRDVAIDMPAGPSEVEVLA
DASANPVFVAADLLSQAEHGVDSQAMLITTSEKLQAEVMEEVNRQLAKLPRREIAAKSLE
NSKLILVKDMDEALELTNAYAPEHLIVETENYLEVAERVINAGSVFLGSLTPESAGDYAS
GTNHTLPTNGYAKAYSGVSLDSFIRKITFQEILPQGMKVIGPAIEEMAANELLDAHKNAV
TVRLNTLK
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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