SitesBLAST
Comparing WP_210399219.1 NCBI__GCF_001579945.1:WP_210399219.1 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)
1karA L-histidinol dehydrogenase (hisd) structure complexed with histamine (inhibitor), zinc and NAD (cofactor) (see paper)
49% identity, 93% coverage: 11:439/463 of query aligns to 3:427/431 of 1karA
- active site: Q256 (= Q268), H259 (= H271), E323 (= E335), H324 (= H336), D357 (= D369), H416 (= H428)
- binding histamine: S137 (= S145), H259 (= H271), D357 (= D369), Y358 (= Y370), H364 (= H376)
- binding zinc ion: H259 (= H271), D357 (= D369)
1kahA L-histidinol dehydrogenase (hisd) structure complexed with l-histidine (product), zn and NAD (cofactor) (see paper)
49% identity, 93% coverage: 11:439/463 of query aligns to 3:427/431 of 1kahA
- active site: Q256 (= Q268), H259 (= H271), E323 (= E335), H324 (= H336), D357 (= D369), H416 (= H428)
- binding histidine: L135 (= L143), H259 (= H271), H324 (= H336), D357 (= D369), Y358 (= Y370), H364 (= H376), E411 (= E423), L413 (= L425), H416 (= H428)
- binding zinc ion: H259 (= H271), D357 (= D369)
1kaeA L-histidinol dehydrogenase (hisd) structure complexed with l- histidinol (substrate), zinc and NAD (cofactor) (see paper)
49% identity, 93% coverage: 11:439/463 of query aligns to 6:430/434 of 1kaeA
- active site: Q259 (= Q268), H262 (= H271), E326 (= E335), H327 (= H336), D360 (= D369), H419 (= H428)
- binding L-histidinol: H262 (= H271), H327 (= H336), D360 (= D369), Y361 (= Y370), H367 (= H376)
- binding nicotinamide-adenine-dinucleotide: F58 (= F63), Y130 (= Y135), P132 (= P137), P162 (= P167), G186 (= G195), P209 (= P218), G210 (= G219), N211 (= N220), F213 (≠ W222), H262 (= H271)
- binding zinc ion: Q259 (= Q268), H262 (= H271), D360 (= D369)
P06988 Histidinol dehydrogenase; HDH; EC 1.1.1.23 from Escherichia coli (strain K12) (see 2 papers)
49% identity, 93% coverage: 11:439/463 of query aligns to 6:430/434 of P06988
- Y130 (= Y135) binding NAD(+)
- Q188 (= Q197) binding NAD(+)
- N211 (= N220) binding NAD(+)
- Q259 (= Q268) binding Zn(2+)
- H262 (= H271) binding Zn(2+)
- D360 (= D369) binding Zn(2+)
- H419 (= H428) 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)
49% identity, 92% coverage: 14:439/463 of query aligns to 9:430/434 of P10370
- H99 (= H104) mutation to N: Slight decrease in activity.
- C117 (= C122) mutation C->A,S: Almost no change in activity.
- C154 (= C159) mutation C->A,S: Almost no change in activity.
- H262 (= H271) mutation to N: 7000-fold decrease in activity.
- H327 (= H336) mutation to N: 500-fold decrease in activity.
- H367 (= H376) mutation to N: Slight decrease in activity.
- H419 (= H428) 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
44% identity, 93% coverage: 10:441/463 of query aligns to 13:433/433 of 6an0A
- active site: Q260 (= Q268), H263 (= H271), E327 (= E335), H328 (= H336), D361 (= D369), H420 (= H428)
- binding histidine: E103 (≠ A109), N104 (≠ E110), K105 (≠ P111), R118 (= R124), E119 (= E125), A120 (≠ F126), K390 (≠ R398)
- binding zinc ion: H263 (= H271), D361 (= D369)
5vldF Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidine and NAD+ (see paper)
46% identity, 92% coverage: 10:436/463 of query aligns to 1:427/435 of 5vldF
- active site: Q258 (= Q268), H261 (= H271), E326 (= E335), H327 (= H336), D360 (= D369), H419 (= H428)
- binding histidine: S135 (= S145), S236 (= S246), Q258 (= Q268), H261 (= H271), E326 (= E335), H327 (= H336), D360 (= D369), Y361 (= Y370), H367 (= H376), E414 (= E423), H419 (= H428)
- binding nicotinamide-adenine-dinucleotide: F55 (= F63), D56 (= D64), Y125 (= Y135), P127 (= P137), G129 (= G139), T130 (≠ V140), Q187 (= Q197), P208 (= P218), G209 (= G219), N210 (= N220), Y212 (≠ W222), A233 (= A243), G234 (= G244), S236 (= S246), H261 (= H271), E326 (= E335), H367 (= H376), V368 (= V377), L369 (= L378)
- binding zinc ion: Q258 (= Q268), H261 (= H271), D360 (= D369)
5vlbA Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with imidazole (see paper)
46% identity, 91% coverage: 15:436/463 of query aligns to 7:426/434 of 5vlbA
5vlcA Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidinol (see paper)
46% identity, 92% coverage: 10:436/463 of query aligns to 1:424/431 of 5vlcA
- active site: Q255 (= Q268), H258 (= H271), E323 (= E335), H324 (= H336), D357 (= D369), H416 (= H428)
- binding L-histidinol: H258 (= H271), E323 (= E335), H324 (= H336), D357 (= D369), Y358 (= Y370), H364 (= H376), E411 (= E423), H416 (= H428)
- binding zinc ion: Q255 (= Q268), H258 (= H271), D357 (= D369)
4g09A The crystal structure of the c366s mutant of hdh from brucella suis in complex with a substituted benzyl ketone (see paper)
46% identity, 86% coverage: 41:439/463 of query aligns to 28:425/432 of 4g09A
- active site: Q253 (= Q268), H256 (= H271), E321 (= E335), H322 (= H336), D355 (= D369), H414 (= H428)
- binding (3S)-3-amino-1-[4-(benzyloxy)phenyl]-4-(1H-imidazol-4-yl)butan-2-one: P126 (= P137), A130 (= A141), Y132 (≠ L143), S134 (= S145), H256 (= H271), E321 (= E335), H322 (= H336), D355 (= D369), Y356 (= Y370), H362 (= H376)
- binding zinc ion: H256 (= H271), D307 (≠ S321), D310 (= D324), D355 (= D369)
Query Sequence
>WP_210399219.1 NCBI__GCF_001579945.1:WP_210399219.1
MTAELRSQLPIRRWSSLSAQERYTALRRPAQRNTQALHEQVREIIQEVRSRGDHALVDYA
RRFDGVELTTLEVTPAEFAAAQTSLDAVQRQALERAIANVRRFHEAQRAEPIRLEISPGV
TCEREFRPIDAVGLYVPAGVAPLPSTAIMLAVPALIAGCPTRIICTPPRKDGSADPAVLT
VARLCGIERVFKLGGAQAIAAMAYGTASVPKVDKVYGPGNAWVTAAKLLVANDPDGAALD
LPAGPSEVLVIADEQAHPEFVAADLLAQTEHSADAQSVLVTTSMALAQATLEQLAAQMPR
LERERTLREAIQNTRLFLVDSLQDAFDLSNTYAPEHLIIQIAAARAWVPQVRNAGSVFLG
AWTPETMGDYCSGTNHVLPTYGFARAYSGLGLGDFLKRITIQELTADGLRDLGPTALTIA
HMEGLGAHANAVQVRLAYLATVLPDGVRAAARPDTPLRGSEGA
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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