SitesBLAST
Comparing CA265_RS03635 FitnessBrowser__Pedo557:CA265_RS03635 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)
6an0A Crystal structure of histidinol dehydrogenase from elizabethkingia anophelis
52% identity, 99% coverage: 6:426/426 of query aligns to 9:430/433 of 6an0A
- active site: Q260 (= Q256), H263 (= H259), E327 (= E323), H328 (= H324), D361 (= D357), H420 (= H416)
- binding histidine: E103 (≠ K100), N104 (≠ T101), K105 (≠ E102), R118 (= R115), E119 (= E116), A120 (≠ S117), K390 (= K386)
- binding zinc ion: H263 (= H259), D361 (= D357)
5vldF Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidine and NAD+ (see paper)
51% identity, 100% coverage: 1:426/426 of query aligns to 2:429/435 of 5vldF
- active site: Q258 (= Q256), H261 (= H259), E326 (= E323), H327 (= H324), D360 (= D357), H419 (= H416)
- binding histidine: S135 (= S136), 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 (= F54), D56 (= D55), Y125 (= Y126), P127 (= P128), G129 (= G130), T130 (= T131), Q187 (= Q188), P208 (= P209), G209 (= G210), N210 (= N211), Y212 (= Y213), 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)
51% identity, 100% coverage: 1:426/426 of query aligns to 1:428/434 of 5vlbA
5vlcA Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidinol (see paper)
50% identity, 100% coverage: 1:426/426 of query aligns to 2:426/431 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)
P10370 Histidinol dehydrogenase; HDH; EC 1.1.1.23 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
47% identity, 99% coverage: 3:424/426 of query aligns to 6:427/434 of P10370
- H99 (= H95) mutation to N: Slight decrease in activity.
- C117 (= C113) mutation C->A,S: Almost no change in activity.
- C154 (= C150) 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
1karA L-histidinol dehydrogenase (hisd) structure complexed with histamine (inhibitor), zinc and NAD (cofactor) (see paper)
48% identity, 99% coverage: 3:424/426 of query aligns to 3:424/431 of 1karA
- active site: Q256 (= Q256), H259 (= H259), E323 (= E323), H324 (= H324), D357 (= D357), H416 (= H416)
- binding histamine: S137 (= S136), 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)
48% identity, 99% coverage: 3:424/426 of query aligns to 3:424/431 of 1kahA
- active site: Q256 (= Q256), H259 (= H259), E323 (= E323), H324 (= H324), D357 (= D357), H416 (= H416)
- binding histidine: L135 (= L134), H259 (= H259), H324 (= H324), D357 (= D357), Y358 (= Y358), H364 (= H364), E411 (= E411), L413 (= L413), H416 (= H416)
- binding zinc ion: H259 (= H259), D357 (= D357)
1kaeA L-histidinol dehydrogenase (hisd) structure complexed with l- histidinol (substrate), zinc and NAD (cofactor) (see paper)
48% identity, 99% coverage: 3:424/426 of query aligns to 6:427/434 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 (= F54), Y130 (= Y126), P132 (= P128), P162 (= P158), G186 (= G186), P209 (= P209), G210 (= G210), N211 (= N211), F213 (≠ Y213), 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)
48% identity, 99% coverage: 3:424/426 of query aligns to 6:427/434 of P06988
- Y130 (= Y126) binding
- Q188 (= Q188) binding
- N211 (= N211) binding
- Q259 (= Q256) binding
- H262 (= H259) binding
- D360 (= D357) binding
- H419 (= H416) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
4g09A The crystal structure of the c366s mutant of hdh from brucella suis in complex with a substituted benzyl ketone (see paper)
42% identity, 93% coverage: 28:424/426 of query aligns to 24:422/432 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 (= P128), A130 (= A132), Y132 (≠ L134), S134 (= S136), H256 (= H259), E321 (= E323), H322 (= H324), D355 (= D357), Y356 (= Y358), H362 (= H364)
- binding zinc ion: H256 (= H259), D307 (≠ N309), D310 (≠ E312), D355 (= D357)
Query Sequence
>CA265_RS03635 FitnessBrowser__Pedo557:CA265_RS03635
MKIYNYTDLSKSKIEELCSRQIEDDKLVEERVTDIISTVKKDGDQALFNFAKAFDKVDLE
KLFLDAEELKSIASNIPAEAKKAIDTAYQNIKTFHQSQLKTEDKIETMPGVMCWRESRPI
EKVGLYIPGGTAVLPSTFLMLATPAIIAGCKEIVVCSPPQNDGKTNCYLAYCAVLLGIEK
VFLIGGAQAVAAMAFGTESVPQVYKIFGPGNRYVTTAKTMVQNKVAIDMPAGPSEVLVIA
DETANPSFIAADLLAQAEHGTDSQAILVATSYQIIAETLKEIENQLNVLPRKDIAAKAIA
NSYAVLAKNLEEAMQFSNEYAPEHLILATEHFQSLIPLITNAGSVFLGNLTPESAGDYAS
GTNHTLPTSGFAKAYSGVSTDAFLKKITFQHLSATGLNNIGRTVEILAAAEGLEAHKNAV
SIRLKN
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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